产品标准

 浓缩液(1mg/1ml) 亲和纯化抗体

产品应用

WB=1:100-500 Elisa =1:200-1000 IP=1:20-100 IHC=1:100-500    （石蜡切片需做抗原修复）

产品介绍

    Laminins are basement membrane components thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Laminin 5 is an isoform composed of three distinct subunits, alpha 3, beta 3 and gamma 2, which are bound to each other in a cross-shaped molecule by disulphide bonds. It is a complex glycoprotein thought to be involved in cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes. It is also involved in signal transduction via tyrosine phosphorylation of pp125-FAK and p80, and differentiation of keratinocytes.
    The laminin alpha 3 subunit is also thought to be a component of laminin 6 and laminin 7.
    mol wt:190kDa(human, rat) 367kDa(mo)
    Other Aliases:
    Laminin alpha 3; LAMA3; LAMNA; Laminin subunit alpha-3; Laminin-5 subunit alpha; Laminin-6 subunit alpha; Laminin-7 subunit alpha; Epiligrin 170 kDa subunit; E170; Epiligrin subunit alpha; Kalinin subunit alpha; Nicein subunit alpha, BM600; LOCS.)

[FUNCTION] Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. [FUNCTION] Laminin-5 is thought to be involved in (1) cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation of pp125-FAK and p80, (3) differentiation of keratinocytes. [SUBUNIT] Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin). [SUBCELLULAR LOCATION] Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named isoforms=2; Name=2; Synonyms=B; IsoId=Q16787-2; Sequence=Displayed; Name=1; Synonyms=A; IsoId=Q16787-1; Sequence=VSP_035738, VSP_035739. [TISSUE SPECIFICITY] Skin; respiratory, urinary, and digestive epithelia and in other specialized tissues with prominent secretory or protective functions. Epithelial basement membrane, and epithelial cell tongue that migrates into a wound bed. A differential and focal expression of the subunit alpha-3 is observed in the CNS. [INDUCTION] Laminin-5 is up-regulated in wound sites of human skin. [DOMAIN] The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. [DOMAIN] Domain G is globular. [DISEASE] Defects in LAMA3 are a cause of epidermolysis bullosa junctional Herlitz type (H-JEB) [MIM:226700]; also known as junctional epidermolysis bullosa Herlitz-Pearson type. JEB defines a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement membrane. H-JEB is a severe, infantile and lethal form. Death occurs usually within the first six months of life. Occasionally, children survive to teens. H-JEB is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic. [DISEASE] Defects in LAMA3 are the cause of laryngoonychocutaneous syndrome (LOCS) [MIM:245660]. LOCS is an autosomal recessive epithelial disorder confined to the Punjabi Muslim population. The condition is characterized by cutaneous erosions, nail dystrophy and exuberant vascular granulation tissue in certain epithelia, especially conjunctiva and larynx. [SIMILARITY] Contains 15 laminin EGF-like domains. [SIMILARITY] Contains 5 laminin G-like domains. [SIMILARITY] Contains 1 laminin IV type A domain. [SIMILARITY] Contains 1 laminin N-terminal domain