VTI1A Protein (AA 1-217) (Strep Tag)

Catalog No. ABIN3075464

Product Details

Target: VTI1A (Vesicle Transport through Interaction with t-SNAREs 1A (VTI1A))

Protein Type: Recombinant

Protein Characteristics: AA 1-217

Origin: Human

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This VTI1A protein is labelled with Strep Tag.

Application: ELISA, Western Blotting (WB), SDS-PAGE (SDS)

Sequence: MSSDFEGYEQ DFAVLTAEIT SKIARVPRLP PDEKKQMVAN VEKQLEEAKE LLEQMDLEVR EIPPQSRGMY SNRMRSYKQE MGKLETDFKR SRIAYSDEVR NELLGDDGNS SENQRAHLLD NTERLERSSR RLEAGYQIAV ETEQIGQEML ENLSHDREKI QRARERLRET DANLGKSSRI LTGMLRRIIQ NRILLVILGI IVVITILMAI TFSVRRH
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us.

Characteristics: Key Benefits:

• Made in Germany - from design to production - by highly experienced protein experts.
• Protein expressed with ALiCE® and purified by multi-step, protein-specific process to ensure correct folding and modification.
• These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

Expression System:

• ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
• During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Concentration:

• The concentration of our recombinant proteins is measured using the absorbance at 280nm.
• The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.
• We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

Purification: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Purity: >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin Level: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Grade: Crystallography grade

Application Details

Application Notes: In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.

Comment:

ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: Unlimited (if stored properly)

Target Details

Target: VTI1A (Vesicle Transport through Interaction with t-SNAREs 1A (VTI1A))

Alternative Name: VTI1A (VTI1A Products)

Synonyms: zgc:109895 Protein, mvti1 Protein, vti1-rp2 Protein, DDBDRAFT_0219803 Protein, DDBDRAFT_0231536 Protein, DDB_0219803 Protein, DDB_0231536 Protein, MMDS3 Protein, MVti1 Protein, VTI1RP2 Protein, Vti1-rp2 Protein, 1110014F16Rik Protein, 1110018K19Rik Protein, 4921537J05Rik Protein, MVti1a Protein, Vti1 Protein, vesicle transport through interaction with t-SNAREs 1A L homeolog Protein, vesicle transport through interaction with t-SNAREs 1A Protein, v-SNARE family protein Protein, vti1a.L Protein, vti1a Protein, VTI1A Protein, vti1A Protein, Vti1a Protein

Background: Vesicle transport through interaction with t-SNAREs homolog 1A (Vesicle transport v-SNARE protein Vti1-like 2) (Vti1-rp2),FUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non-conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2. May be involved in increased cytokine secretion associated with cellular senescence. {ECO:0000269|PubMed:18195106, ECO:0000269|PubMed:19138172}.

Molecular Weight: 25.2 kDa

UniProt: Q96AJ9