Recombinant Human S100A9 Protein

Name: Recombinant Human S100A9 Protein
Brand: Beta LifeScience
SKU: BLPSN-4136
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	NP_002956.1
Synonym	60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP-14, MRP14, NIF, P14
Background	S1 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S1 proteins, and the name is derived from the fact that the protein is 1% soluble in ammonium sulfate at neutral pH. Most S1 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S1 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S1-A9, also known as S1 calcium-binding protein A9, S1A9, and CAGB, is a member of the S-1 family. S1A9 is expressed by macrophages in acutely inflammed tissues and in chronic inflammation. It is also expressed in epithelial cells constitutively or induced during dermatoses. S1A9 is a calcium-binding protein. It has anti-microbial activity towards bacteria and fungi. The anti-microbial and proapoptotic activity of S1A9 is inhibited by zinc ions. S1A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when unphosphorylated. It also promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S1A9 plays a role as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
Description	A DNA sequence encoding the native form of human S100A9 (NP_002956.1) (Met 1-Pro 114) was expressed.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Met 1-Pro 114
Molecular Weight	The recombinant human S100A9 consisting of 114 a.a. and migrates with an apparent molecular mass of 26 & 13 kDa corresponding to dimeric and monomeric form as estimated in SDS-PAGE under Non-reduced condition.
Purity	>95% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.