Biotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14) 8021

Additional Information:
accession P16627|express systemE.coli|product tagbiotin at C-terminal|purity> 97% by SDS PAGE|molecular weightPredicted Molecular Mass: 10,219.5471 Da Extinction Coefficient: 19,300 M-1 cm-1 Actual Molecular Mass: 10,219.5471 Da by ESI Mass Spec|available size10 g, 100 g, 2 g, 50 g|endotoxinBiotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14) 8021proteinDatabase link:human P16627 Size and concentration2, 10, 50, 100g and lyophilizedFormLyophilizedStorage InstructionsAvoid repeated freeze-thaw cycles: 12 months from date of receipt, -20 to -70 C as supplied. 1 month, 2 to 8 C under sterile conditions after reconstitution. 3 months, -20 to -70 C under sterile conditions after reconstitutionStorage bufferReconstitution: Spin sample prior to reconstitution. Recommended concentration of 100g/mL in sterile water.Shipping: Room TempPurity> 97% by SDS PAGE and HPLCtarget relevanceHemofiltrate CC chemokine-1(HCC-1/CCL14) is endogeneously expressed by numerous tissues. Upon processing of the N terminal residues of the full length HCC-1 by the uPA-plasmin system, the active form of HCC-1 is a strong agonist for CCR1, CCR5 and to a lesser extent CCR3, and causes chemotaxis of different types of leukocytes. The active form of HCC-1 is also shown as a potent inhibitor of HIV entry.Protein namesHeat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa-like protein 1) (Spermatid-specific heat shock protein 70)Gene namesHspa1l,Hspa1l Hsc70tProtein familyHeat shock protein 70 familyMass70637DaFunctionMolecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria.TissuesExpressed in spermatids.StructureInteracts with PRKN.DomainThe N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsiTarget Relevance information above includes information from UniProt accession: P16627The UniProt Consortium|