Human DST - Recombinant Protein | Custom Made-To-Order

Name: Human DST (Dystonin) - Recombinant Protein
Brand: Beta LifeScience
SKU: BLT-07949P
Price: 445.0 USD
Availability: InStock

SDS-PAGE analysis of Human DST (Dystonin) - Recombinant Protein, CAT# BLT-07949P, showing >90% purity under 15% SDS-PAGE (Reduced)

Price Save $150

Size

100ug

Quantity

Quantity Pricing

Pack Size	Price (USD)
500 µg	$1,030 (Fall Promotion)
1 mg	$1,870 (Fall Promotion)

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Product Overview

Product Name	Recombinant Human Dystonin (DST) Protein
Product Overview	This recombinant human Dystonin (DST) protein includes amino acids 1-252aa of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in PBSprior to lyophilization.
Target Uniprot Id	Q03001
Recommended Name	Dystonin
Gene Name	DST
Synonyms	BP240; BPA; BPAG1; CATX-15; DMH; MACF2; Dystonia musculorum protein; Bullous Pemphigoid Antigen 1; H
Species	Human
Predicted Molecular Mass	28 kDa
Expression System	E.coli
Expression Range	1-252aa
Tag	N-6His
Purity	>90%
Formulation	Lyophilized
Buffer	PBS
Storage Condition	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Reconstitution Instruction	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Applications	Positive Control; Immunogen; SDS-PAGE; WB
Research Area	Signal Transduction
Target Function	Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1.; plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.; required for bundling actin filaments around the nucleus.; regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.
Subcellular Location	Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber. Cell projection, axon.; [Isoform 1]: Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, H zone.; [Isoform 2]: Cytoplasm, cytoskeleton.; [Isoform 3]: Cytoplasm, cytoskeleton. Cell junction, hemidesmosome.; [Isoform 6]: Nucleus. Nucleus envelope. Membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber.; [Isoform 7]: Cytoplasm, cytoskeleton. Cell projection, axon. Membrane. Note=Associates with axonal microtubules and intermediate filaments, but not with actin cytoskeleton, in sensory neurons.; [Isoform 8]: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Cell membrane; Lipid-anchor.
Associated Diseases	Neuropathy, hereditary sensory and autonomic, 6 (HSAN6); Epidermolysis bullosa simplex, autosomal recessive 2 (EBSB2)
Tissue Specificity	Isoform 1 is expressed in myoblasts (at protein level). Isoform 3 is expressed in the skin. Isoform 6 is expressed in the brain. Highly expressed in skeletal muscle and cultured keratinocytes.

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FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.