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HAS2 Antibody (Center)

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
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  • 1 - HAS2 Antibody (Center) AW5442
    All lanes : Anti-HAS2 Antibody (Center) at 1:1000 dilution Lane 1: human heart lysates Lane 2: mouse heart lysates Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L),Peroxidase conjugated at 1/10000 dilution Predicted band size : 64 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession Q92819
Other Accession NP_005319.1
Reactivity Human, Mouse
Predicted Rat
Host Rabbit
Clonality Polyclonal
Calculated MW H=64;M=64; R=64 KDa
Isotype Rabbit Ig
Antigen Source HUMAN
Additional Information
Gene ID 3037
Antigen Region 138-166
Other Names Hyaluronan synthase 2, Hyaluronate synthase 2, Hyaluronic acid synthase 2, HA synthase 2, HAS2
Dilution WB~~1:1000
Target/Specificity This HAS2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 138-166 amino acids from the Central region of human HAS2.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsHAS2 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name HAS2
Function Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction and it is particularly responsible for the synthesis of high molecular mass hyaluronan. Required for the transition of endocardial cushion cells into mesenchymal cells, a process crucial for heart development. May also play a role in vasculogenesis. High molecular mass hyaluronan also play a role in early contact inhibition a process which stops cell growth when cells come into contact with each other or the extracellular matrix (By similarity).
Cellular Location Membrane; Multi-pass membrane protein
Tissue Location Expressed in fibroblasts.
Research Areas

BACKGROUND

Hyaluronan or hyaluronic acid (HA) is a high molecular weight unbranched polysaccharide synthesized by a wide variety of organisms from bacteria to mammals, and is a constituent of the extracellular matrix. It consists of alternating glucuronic acid and N-acetylglucosamine residues that are linked by beta-1-3 and beta-1-4 glycosidic bonds. HA is synthesized by membrane-bound synthase at the inner surface of the plasma membrane, and the chains are extruded through pore-like structures into the extracellular space. It serves a variety of functions, including space filling, lubrication of joints, and provision of a matrix through which cells can migrate. HA is actively produced during wound healing and tissue repair to provide a framework for ingrowth of blood vessels and fibroblasts. Changes in the serum concentration of HA are associated with inflammatory and degenerative arthropathies such as rheumatoid arthritis. In addition, the interaction of HA with the leukocyte receptor CD44 is important in tissue-specific homing by leukocytes, and overexpression of HA receptors has been correlated with tumor metastasis. HAS2 is a member of the newly identified vertebrate gene family encoding putative hyaluronan synthases, and its amino acid sequence shows significant homology to glycosaminoglycan synthetase (DG42) from Xenopus laevis, and human and murine hyaluronan synthase 1.

REFERENCES

Simpson, M.A., et al. J. Biol. Chem. 277(12):10050-10057(2002) Spicer, A.P., et al. Biochem. Soc. Trans. 27(2):109-115(1999) Spicer, A.P., et al. Genomics 41(3):493-497(1997) Watanabe, K., et al. J. Biol. Chem. 271(38):22945-22948(1996)

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