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Brand: ProteoGenix

Recombinant Human LAMB3 Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
67.24 kDa

329.00

+ 329 loyalty points
Thr587–Lys1172
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Recombinant Human LAMB3 Protein, N-His

Recombinant Human LAMB3 Protein, N-His

Product name Recombinant Human LAMB3 Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 67.24 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Thr587-Lys1172
Aliases /Synonyms Laminin subunit beta-3, Epiligrin subunit bata, Kalinin B1 chain, Kalinin subunit beta, Laminin B1k chain, Laminin-5 subunit beta, Nicein subunit beta, LAMB3, LAMNB1, laminin-5, laminin-332, epiligrin, kalinin, nicein
Reference ARO-P11460
Note For research use only.
Molecular Constructor
Thr587–Lys1172

The Structure and Function of Recombinant Human LAMB3 Protein

Recombinant human LAMB3 protein, also known as laminin subunit beta-3, is a member of the laminin family of proteins. Laminins are large, multidomain glycoproteins that play a crucial role in cell adhesion, migration, and differentiation. LAMB3 is a key component of the basement membrane, a specialized extracellular matrix that provides structural support and signaling cues to cells.

Structure of Recombinant Human LAMB3 Protein

The LAMB3 gene is located on chromosome 1 and encodes a protein of 1,590 amino acids. The primary structure of LAMB3 is characterized by a series of distinct domains, including a short N-terminal domain, a laminin N-terminal (LN) domain, several epidermal growth factor (EGF)-like repeats, and a C-terminal globular domain. These domains are connected by flexible linker regions, allowing for conformational changes and interactions with other proteins.

The LN domain of LAMB3 is responsible for binding to other laminin subunits, forming a heterotrimeric complex with laminin alpha and gamma subunits. This complex is further stabilized by disulfide bonds between the LN domains of each subunit. The EGF-like repeats of LAMB3 provide binding sites for integrin receptors, which mediate cell adhesion and signaling. The C-terminal globular domain of LAMB3 is involved in interactions with other extracellular matrix components, such as collagen and heparin sulfate proteoglycans.

Activity of Recombinant Human LAMB3 Protein

The main function of LAMB3 is to promote cell adhesion and migration by forming a stable network of interactions between cells and the extracellular matrix. This is achieved through its binding to integrin receptors and other laminin subunits. LAMB3 is also involved in regulating cell differentiation and survival by activating signaling pathways through its interactions with growth factor receptors.

Defects in the LAMB3 gene can lead to a rare genetic disorder known as Herlitz junctional epidermolysis bullosa (H-JEB). This condition is characterized by severe blistering of the skin and mucous membranes due to a weakened basement membrane. Recombinant human LAMB3 protein has been used in preclinical studies to restore the structural integrity of the basement membrane and improve the symptoms of H-JEB.

Applications of Recombinant Human LAMB3 Protein

Recombinant human LAMB3 protein has a wide range of applications in both research and therapeutic settings. In research, it is used as a tool to study the structure and function of laminins and their role in cell adhesion, migration, and differentiation. Recombinant LAMB3 can also be used to generate antibodies for detecting and quantifying LAMB3 protein levels in biological samples.

In the clinic, recombinant LAMB3 has been investigated as a potential treatment for H-JEB and other conditions characterized by defects in the basement membrane. Preclinical studies have shown promising results, and clinical trials are currently underway to evaluate the safety and efficacy of recombinant LAMB3 protein therapy in patients with H-JEB.

In summary, recombinant human LAMB3 protein is a key component of the basement membrane, playing a crucial role in cell adhesion, migration, and differentiation. Its structural and functional properties make it a valuable tool for research and a potential therapeutic agent for various diseases. Further studies on the structure and activity of LAMB3 will continue to enhance our understanding of its role in health and disease.

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