2% Hemoglobin Solution - BioReagent

Cat. No.: H1528586

GRADE & PURITY BioReagent

Storage

Store at 2-8°C

Shipped In

Wet ice

Overview

For use as an isolation medium for Neisseria.

Specifications

Specifications & Purity

BioReagent

Storage

Store at 2-8°C

Shipped In

Wet ice

This product requires cold chain shipping. Ground and other economy services are not available.

Grade

BioReagent

Product Line

Biological Products

Application Protocols

Not specified for this item; refer to CoA/Spec Sheet and the product SDS for any handling notes.

General note: While hemoglobin solutions are commonly used in spectrophotometric demonstrations and ligand-binding studies, no validated, product-specific protocols or recommended dilutions are provided in the Product Data.

Biological Roles

General biology of hemoglobin (literature; not product specifications)

• Primary function: Reversible transport of oxygen from respiratory organs to tissues, and facilitation of CO2 carriage (as carbamates) and H+ buffering (Bohr effect) via allosteric transitions between T and R states.
• Structure–function: Tetrameric α2β2 assembly with cooperative O2 binding; heme Fe(II) binds O2, while the protein environment tunes affinity and reactivity. Redox cycling to Fe(III) yields methemoglobin, which lacks O2-binding capability.
• Allosteric effectors: pH/CO2, chloride, and organic phosphates (e.g., 2,3-BPG in mammals) modulate affinity; mutations affect stability/affinity (basis of many hemoglobin variants).
• Spectroscopy: Distinct absorption signatures enable noninvasive optical measurements in research (e.g., oximetry models) and are widely used in teaching labs.
• Enzymatic side activities: Exhibits pseudoperoxidase activity with H2O2 and can scavenge/react with NO and other diatomics, influencing redox signaling in vitro.

Relevance to laboratory research

• Serves as a robust, well-characterized model protein to study cooperativity, ligand binding, electron transfer, and protein stability.
• Useful as a standard in heme quantification assays and as a comparator for other hemoproteins (e.g., myoglobin, cytochromes).

Note: The above describes the native biomolecule broadly. Source organism, post-translational modifications, and any processing for this product are not specified; consult CoA/Spec Sheet if these details are critical to your application.

Buffer Applications

Not typically applicable. Hemoglobin is not used as a buffering agent. Instead, it is a protein analyte/system studied within buffers.

Practical notes (general)

• Typical working pH: Near neutral (pH ~7–8) to preserve structure and native spectra (literature). Exact buffer composition of this item is not specified; refer to CoA/Spec Sheet.
• Common compatible buffers: Phosphate, HEPES, or Tris are frequently used for hemoglobin studies. Buffer selection can influence oxygen affinity and redox stability; maintain consistency across experiments.
• Ionic strength/osmolytes: Moderate ionic strength and mild osmolytes (e.g., glycerol at low percentages) may stabilize structure; evaluate empirically.

For electrophoresis or chromatography, hemoglobin can serve as a protein standard/analyte, but the solution’s formulation details (salt, pH, additives) are required to design buffer systems—these are not specified for this item.

Green Alternatives

Applicability

• As a ready-to-use aqueous protein solution, conventional “green solvent” substitution is not directly relevant. However, sustainability considerations can still guide experimental choices.

Options and trade-offs (general guidance)

• Use minimal volumes and right-size aliquots to reduce cold-chain shipping/storage demands.
• When feasible, select recombinant or non-animal–derived hemoglobin for reduced animal sourcing impact (if functionally acceptable for your study). This product’s source is not specified; refer to CoA/Spec Sheet.
• Consider lyophilized hemoglobin preparations for room-temperature shipment and reconstitution on site, balancing convenience with potential changes in spectral/functional properties upon rehydration.
• For heme chemistry in organic media, hemin or synthetic porphyrins can replace protein solutions, eliminating refrigeration but sacrificing native allosteric behavior.

Simple comparison (context; not product-specific)

• 2% hemoglobin solution: Ready-to-use, minimal prep, requires 2–8 °C cold chain; protein waste requires aqueous biowaste handling.
• Lyophilized hemoglobin: Lower shipping mass/energy, reconstitution generates plastic/buffer waste; may require optimization to match native spectra.
• Heme model compounds: No cold chain, compatible with greener solvents; reduced biological relevance to globin-mediated effects.

Pharmaceutical Uses

This product is labeled For research use only and is not intended for human or veterinary use, diagnostic procedures, or as a drug substance.

Research/formulation context (general; not product-specific)

• Model protein: Hemoglobin solutions are sometimes used as surrogates in formulation/process development studies to evaluate protein stability, device extraction/leachables, or optical methods because of well-defined spectra.
• Excipient status: Hemoglobin is not a typical excipient. Any use in pharmaceutical manufacturing would require defined sourcing, quality, and regulatory status—not specified for this item.
• Compendial status: No pharmacopeial monograph is implied by the BioReagent grade. If a compendial grade is required, consult pharmacopeial references and source accordingly.

Regulatory note

• For any GMP or clinical application, obtain materials with appropriate documentation (CoA, TSE/BSE statements, viral safety, bioburden/endotoxin limits). Such controls are not specified for this product.

Physical Properties

Item-specific

• Concentration: 2% solution (nominal). Exact protein concentration, buffer identity, pH, and additives: Not specified for this item; refer to CoA/Spec Sheet.
• Density, refractive index, viscosity, exact pH: Not specified for this item; refer to CoA/Spec Sheet.

Literature/typical values for hemoglobin (for context only; not product specifications)

• Molecular weight: ~64.5 kDa for the α2β2 tetramer (literature).
• Isoelectric point (pI): ~6.8–7.0 (species- and preparation-dependent; literature).
• Solubility: Highly soluble in aqueous buffers; precipitation near pI or under denaturing/oxidizing conditions (literature).
• Spectral features: Strong Soret band near ~415 nm; oxyhemoglobin Q-bands near ~541 and ~576 nm; deoxy- and met- forms show shifted/altered bands (literature). Useful for spectrophotometer calibration and redox/ligand-binding assays.
• Redox/ligand states: Fe(II) binds O2, CO, NO; oxidation to Fe(III) yields methemoglobin, which does not bind O2 (literature).
• Thermal sensitivity: Denatures upon heating; typical unfolding onset below 70 °C depending on buffer and concentration (literature). Avoid elevated temperatures during handling.

Compatibility notes (general)

• Compatible with most neutral aqueous buffers (e.g., phosphate, HEPES, Tris). High oxidant levels, extremes of pH, strong denaturants (urea, guanidinium), or organic cosolvents can alter spectra and activity.

Quality & Grades

Item-specific

• Grade: BioReagent (from Product Data). Intended for research use only; not for human or veterinary use.

What BioReagent grade generally implies (context; not a specification)

• Prepared to support common biochemical and life-science experiments (e.g., spectrophotometry, teaching labs, biochemical assays) with attention to functional integrity and low levels of common contaminants that would interfere with typical research workflows.
• May emphasize clarity, reliable spectral behavior, and batch-to-batch consistency. Exact acceptance criteria (e.g., methemoglobin content, protein concentration tolerance, residual salts, microbial limits) are not specified for this item; refer to CoA/Spec Sheet for lot-specific metrics.

Stabilizers and additives

• Any stabilizers, buffer composition, or preservatives (e.g., salts, pH, antimicrobial agents) are not specified for this item; refer to CoA/Spec Sheet. The presence/absence of preservatives can affect spectral properties and compatibility with downstream assays.

Practical notes for users

• Verify concentration and oxidation state upon receipt if your application requires a defined oxy-/deoxy-/met-state.
• Record lot number in your ELN; spectral fingerprints (Soret and Q-bands) provide a quick QC check of state and integrity.
• For highly sensitive enzymatic or heme-reactivity studies, consider running blanks with the supplied buffer to account for any background absorbance.

Reaction & Applications

Item-specific applications: Not explicitly specified for this item; refer to catalog/CoA. The following are common research uses of hemoglobin solutions (literature/general):

Analytical and teaching uses

• Spectrophotometer calibration and demonstration of ligand-dependent spectra (oxy vs deoxy vs methemoglobin). Monitor Soret (~415 nm) and Q-bands (~541/576 nm for oxyHb).
• Oxygen-binding kinetics and equilibria: Measure O2 dissociation curves, Hill coefficient, effects of pH/CO2 (Bohr effect) and allosteric effectors (e.g., 2,3-BPG where applicable).

Biochemical/chemical reactivity

• Pseudoperoxidase assays: Hemoglobin exhibits peroxidase-like activity with H2O2; useful as a heme protein comparator (exercise caution with oxidants).
• Ligand-binding/selectivity studies with CO, NO, CN−, and small-molecule heme ligands.
• Redox interconversions: Controlled oxidation (metHb formation) and reduction (restoring Fe(II)) for method development.

Practical tips

• Work cold and minimize light/air exposure if maintaining a defined redox/ligand state; sparge buffers with N2/Ar for deoxyHb work. Use gas-tight cuvettes for CO/NO binding studies.
• Verify concentration by UV–vis using literature extinction behavior; confirm state by spectral positions, not just intensity.
• Avoid contaminating heme pocket with high concentrations of detergents or denaturants unless unfolding is intended for study.

Reaction Conditions

No specific reaction conditions are provided for this item. The following are general laboratory conditions for common hemoglobin manipulations (literature; not product specifications):

• Oxy ↔ deoxy interconversion: Work in phosphate/HEPES buffer at pH ~7.0–7.4, 2–8 °C. Deoxygenate by sparging with N2/Ar and adding a mild reductant (e.g., sodium dithionite) as appropriate; re-oxygenate by air equilibration. Monitor at 415/541/576 nm.
• Methemoglobin formation: Gentle oxidation with ferricyanide or controlled H2O2 exposure at 0–4 °C; remove excess oxidant by desalting. Verify metHb by the characteristic spectrum (Soret shift, altered Q-bands).
• Ligand binding (CO/NO): Use gas-tight cuvettes/syringes; perform under a fume hood with strict safety controls. Low micromolar to sub-millimolar Hb in neutral buffer; temperature 4–25 °C. Track spectral shifts in real time.
• Stability studies: Thermal ramps (e.g., 20–70 °C) with circular dichroism or UV–vis to detect unfolding/aggregation; avoid prolonged high temperatures.

Cautions

• Oxidants/reductants and gaseous ligands pose safety risks—follow institutional SOPs. Reaction additives can irreversibly modify heme or globin; pilot small-scale tests first.

Item note: Exact composition and allowable storage/handling constraints for this product are not specified; consult the CoA/Spec Sheet and SDS before applying any of the above procedures.

Safety & Handling

Item-specific

• GHS classification, signal word, hazard statements, pictograms: Not specified for this item; refer to the SDS.
• Storage: Store at 2–8 °C (from Product Data). Shipped on wet ice.

General guidance (not a substitute for SDS)

• Expected hazards: Protein aqueous solutions are generally of low acute toxicity, but treat as a laboratory chemical. Composition (e.g., buffer salts, potential preservatives) is not specified for this item; consult CoA/SDS for any biocides or allergens.
• PPE: Wear lab coat, safety glasses, and disposable gloves. Avoid aerosol generation and ingestion. Work on a clean surface; keep container closed when not in use.
• First aid (general): In case of contact with eyes/skin, rinse with water. If inhaled (aerosols), move to fresh air. If ingested, rinse mouth and seek medical advice. Always follow institutional biosafety policies.
• Handling tips: Keep cold during use to minimize denaturation and oxidative conversion to methemoglobin. Avoid repeated freeze–thaw unless the SDS/CoA recommends freezing; many protein solutions lose functionality upon cycling.
• Incompatibilities: Strong oxidizers, strong acids/bases, and proteolytic enzymes can degrade or modify hemoglobin. Metal chelators, nitrites/nitrates, and reducing/oxidizing agents can shift redox/ligand states—use only if intended.
• Waste: Dispose according to local regulations for aqueous biological/chemical waste. Deactivate any preservatives per SDS before drain disposal if permitted.

Solvent Selection

Not typically applicable. This product is itself an aqueous 2% hemoglobin solution, not a solvent for synthetic chemistry.

General compatibility notes (for experimental planning)

• Matrix: Aqueous buffer (exact identity not specified for this item; refer to CoA/Spec Sheet).
• Miscibility: Fully miscible with water and typical biological buffers. Addition of significant organic solvent fractions (e.g., >10–20% v/v ethanol, methanol, acetonitrile) can denature or alter spectra; evaluate case-by-case.
• pH: Hemoglobin is most stable near neutral pH; deviations can change redox/ligand equilibria and promote denaturation (literature guidance).
• Alternatives: For studies requiring organic-rich media, consider heme model compounds (e.g., hemin) that better tolerate nonaqueous conditions, understanding these lack the native globin environment.

Storage & Reconstitution

Item-specific

• Storage: Store at 2–8 °C (from Product Data). Shipments are on wet ice.
• Reconstitution: Not applicable; the product is supplied as a ready-to-use aqueous solution. If a specific working concentration is required, dilute with a compatible buffer. Exact buffer identity and pH of the stock are not specified; refer to CoA/Spec Sheet.

General handling guidance (not product specifications)

• Avoid freezing unless the CoA/SDS explicitly supports it; many protein solutions lose activity or aggregate upon freeze–thaw.
• Aliquot upon first use to minimize repeated temperature cycling and potential microbial contamination if no preservative is present (presence/absence of preservatives not specified for this item).
• Protect from excessive light and air exposure if maintaining a defined oxy-/deoxy-state is important to your application. Work on ice during manipulations.
• Record opening date and store in clean, sealed containers. For long-term storage, consult the CoA for shelf-life and any recommended stabilizers.

Research Use Only

• Labeled for research use only; not for diagnostic or therapeutic use.

Structure & Identity

Item-specific (from Product Data)

• Product name: 2% Hemoglobin Solution (SKU H1528586)
• Grade: BioReagent
• Physical form: Aqueous solution (2% w/v nominal; exact composition not specified for this item; refer to CoA/Spec Sheet.)
• CAS, SMILES, InChIKey, CID, Molecular formula, Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.

General structural description (literature)

• Hemoglobin is a tetrameric globular protein typically composed of two α and two β subunits (α2β2 in adult human HbA). Each subunit is ~16 kDa and binds one protoheme IX (heme) cofactor containing Fe(II) at its center.
• Overall quaternary structure: roughly spheroidal tetramer with cooperative oxygen-binding interfaces (T ↔ R states).
• Key functional groups: Porphyrin macrocycle (conjugated tetrapyrrole), iron coordination sphere (proximal histidine ligand, distal pocket for O2/CO/NO), numerous ionizable side chains contributing to Bohr effect.
• Post-translational features: In erythrocytes, hemoglobin may undergo reversible ligand binding (O2, CO2 as carbamates, NO) and redox cycling between oxyHb, deoxyHb, and metHb (Fe(III)).
• 2D depiction (verbal): Four polypeptide chains folded into α-helical bundles surrounding a planar heme; the iron is centrally positioned within the porphyrin, coordinated axially to His F8 (proximal) and capable of binding small diatomic ligands on the distal side.

Synthetic Utility

Not a small-molecule building block. As a protein solution, hemoglobin has no direct role in classical organic synthesis or materials monomer chemistry.

Biochemical/analytical “utility” (general)

• Heme-centered reactivity: Provides a native porphyrin–iron environment for studying small-molecule binding (O2, CO, NO, CN−) and redox reactions under physiologically relevant conditions.
• Calibration/assay standard: Serves as a chromophoric protein standard due to prominent Soret/Q-bands, useful for instrument checks and method development in spectrophotometry.
• Comparative enzymology: Acts as a reference hemoprotein for benchmarking peroxidase-like activity in mechanistic studies.

Retrosynthetic/derivatization notes

• Chemical modifications (e.g., crosslinking, PEGylation, site-specific labeling) can be explored on hemoglobin for bioconjugation method development. Such transformations alter function/spectra and should be validated with UV–vis and, when relevant, MS or SDS-PAGE.

Item-specific constraints

• The exact buffer, concentration accuracy, and additive profile are not specified for this item; these factors impact derivatization chemistry and should be verified via CoA/Spec Sheet before planning modifications.

Target Specificity

Not applicable. This product is a 2% hemoglobin protein solution and is not an antibody or affinity reagent. No antigen, clone, isotype, or species reactivity information applies.