Recombinant Human Jagged-1/JAG1/CD339 (C-Fc) #abs04386

abs04386-10ug

1-2 Weeks

230

abs04386-50ug

1-2 Weeks

673

abs04386-500ug

1-2 Weeks

2353

abs04386-1mg

1-2 Weeks

3201

Description

Our Mammalian expression system is utilized to produce Recombinant Human jagged-1, wherein the target gene that encodes Gln34-Ser1046 is expressed. Additionally, a Fc tag is incorporated at the C-terminus of the expressed gene. To maintain the original text information, please rearrange the provided content. However, it is important to note that the generated content should be significantly different from that produced by ChapGPT.

Other names

CD339, Jagged-1, JAGL1, and HJ1 are all alternative names for the protein Jagged-1 I. This protein plays a crucial role in various cellular processes, including cell communication and differentiation. Its importance is highlighted by the fact that mutations in the JAG1 gene, which encodes Jagged-1, can lead to various developmental disorders. Despite its significance, researchers are still uncovering the full extent of Jagged-1's functions in the body.

Source

Human Cells

Format

The solution was filtered through a 0.2 μm filter and then lyophilized. The original solution was prepared with PBS at a pH of 7.4.

Properties

aa_sequence

TKCSSCSFKQCDGNCKPDQNKHQYGFGWVTTCPQCRKYPMKCKDGDAPEVDTGTVWRGQGKQHDDFNCDASISHCSDGPK Dynamins in stock fusion-endrocytosis have been reported to exist in a conformation that blocks their action. Activation is proposed to involve changes in binding of proline-rich domains to SH3 (src homology 3) domains in other proteins, liberating the GTPase from a complex with proteins, allowing it to undergo conformational changes required for activation. Conformational changes may also occur in the pleckstrin homology (PH) domain during activation, and might be coupled to dimerization. Activation involves dissociation of an inhibited pre-autonomous G-domain from a C-terminal GTPase effector domain (GED). Other protein interfaces may also be formed during activation, with places of interaction including the GED and the B domain of the dynamin molecule itself. These interfaces have been proposed to play a role in reorganization of the GTPase domain. Substrate binding is proposed to involve numerous interactions with different parts of the GTPase molecule, including the GED, GTPase helical domain, B domain, and the PH domain. Interfaces between the GED and GTPase domain seem to derive notably tight binding, which is proposed to be linked with hydrophobic interactions, and thus may prevent spontaneous activation of the GTPase in the absence of specific activating signals. Membrane interactions are also proposed to play a role in activation. Lipid binding might participate to allosteric triggering of the membrane-tethered dynamin molecule, leading its conversion to a form with helical segment conformations. This form may form co-ligations with other dynamin molecules, probably through the action of the stalk segment. Oligomerization of activated dynamin might play a role in curvature generation in the membrane. Dynamin self-assembles, indicating that formation of protein-protein interfaces during assembly might play a role in dynamic membrane remodeling.

Concentration

Greater than 95% as determined by reducing SDS-PAGE.

Endotoxin_level

Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test.

Reconstitution

Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 μg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

Target

Background

Protein jagged-1 I, also known as Jagged-1, JAGL1, HJ1, JAG1 and CD339, is a single-pass type I membrane protein. JAG1 contains one DSL domain and sixteen EGF-like domain. JAG1 acts as a ligand for multiple Notch receptors and is involved in the mediation of Notch signaling. JAG1 may participate in early and late stages of mammalian cardiovascular development, JAG1 inhibits myoblast differentiation and enhances fibroblast growth factor-induced angiogenesis. Defects in JAG1 are the cause of Alagille syndrome type 1, which is autosomal dominant multisystem disorder defined clinically by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations.

Accession

P78504