Search: 1000 results found for "CDNF"

Description:

GRO-gamma, CINC-2 beta Rat Recombinant (CXCL3)

Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma (1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.

Product # :

CHM-273

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

GRO-g Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a total molecular mass of 7.8kDa. GRO-g is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.

Purity

Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human CXCR2 transfected 293 cells using a concentration range of 10-100ng/ml.

More Info

Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
Synonyms
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma (1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GRO-g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GRO-g should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GRO-g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSPSL.
Background
What is the molecular weight/Mw of CXCL3 RAT BETA Protein?
CXCL3 RAT BETA Protein has a total Mw of 7.8kDa.

What is the source or expression system of CXCL3 RAT BETA Protein?
Escherichia Coli.

What is the Purity of CXCL3 RAT BETA Protein?
CXCL3 RAT BETA Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL3 RAT BETA Protein?
Determined by its ability to chemoattract human CXCR2 transfected 293 cells using a concentration range of 10-100ng/ml.

What is the amino acid sequence of CXCL3 RAT BETA Protein?
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSPSL.

What applications can CXCL3 RAT BETA Protein be used in?
CXCL3 RAT BETA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL3 RAT BETA Protein?
The endotoxin level is minimal, CXCL3 RAT BETA Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Monocyte Chemotactic Protein-3 Mouse Recombinant (CCL7)

Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.

Product # :

CHM-318

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Monocyte Chemotactic Protein-3 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 74 amino acids and having a molecular mass of 8510 Dalton. The MCP-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity as determined by the ability of Mouse MCP-3 to chemoattract Balb/C mouse spleen MNCs at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

More Info

Introduction
Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3 (MCP3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature protein, it is classified among the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, in a large cluster containing many other CC chemokines and is most closely related to CCL2(previously called MCP1).
Synonyms
Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL7 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Monocyte Chemotactic Protein-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDGPNASTC CYVKKQKIPK RNLKSYRRIT SSRCPWEAVI FKTKKGMEVC AEAHQKWVEE AIAYLDMKTP TPKP.
Background
What is the molecular weight/Mw of CCL7 MOUSE Protein?
CCL7 MOUSE Protein has a total Mw of 8.51kDa.

What is the source or expression system of CCL7 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL7 MOUSE Protein?
CCL7 MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL7 MOUSE Protein?
The specific activity as determined by the ability of Mouse MCP-3 to chemoattract Balb/C mouse spleen MNCs at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL7 MOUSE Protein?
QPDGPNASTC CYVKKQKIPK RNLKSYRRIT SSRCPWEAVI FKTKKGMEVC AEAHQKWVEE AIAYLDMKTP TPKP.

What applications can CCL7 MOUSE Protein be used in?
CCL7 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL7 MOUSE Protein?
The endotoxin level is minimal, CCL7 MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cysteine Dioxygenase Human Recombinant

Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.

Product # :

ENZ-449

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CDO1 Human Recombinant fused with a 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-170 a.a.) and having a molecular mass of 23.9kDa.The CDO1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CDO1 solution contains 20mM Tris buffer(pH 8.0), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
CDO1 (Cysteine dioxygenase) is a mammalian non-heme iron enzyme that initiates a number of significant metabolic pathways associated with pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels. CDO1 is highly expressed in the liver and placenta. On the other hand CDO1 has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells.
Synonyms
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CD55 (38-96 a.a.) Human Recombinant

Cd55, cd-55, daf.

Product # :

PRO-2832

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

The CD55 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CD55 His-Tagged Fusion Protein, produced in E. coli, is a 11kDa protein containing 59 amino acid residues of the CD55Human, 38-96 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Synonyms
Cd55, cd-55, daf.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized CD55 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
CD55 is a part of the RCA family characterized by 4-30 SCRs (short consensus repeats) in their plasma-exposed regions. CD55 is expressed mainly in malignant tumors and nevertheless functions as an inhibitor of the complement system. CD55 attaches to the cell membrane through glycophosphatidylinositol (GPI) anchor and acts as a receptor of various enteroviruses such as coxsackieviruses.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cystatin SN Human Recombinant

Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.

Product # :

PRO-1006

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CST1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (21-141 a.a.) and having a molecular mass of 16.9kDa. CST1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CST1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Cystatin-SN (CST1) belongs to the type 2 salivary cystatin family found in a variety of fluids and secretions, including plasma, tears, and saliva. The cystatin superfamily includes proteins which contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, whereas others have lost or possibly never developed this inhibitory activity. CST1 is up-regulated in cancerous lesions of gastric cancer tissues compared to noncancerous regions, in addition clinicopathological analysis revealed a significant correlation between high expression of CST1.
Synonyms
Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMWSPKEE DRIIPGGIYN ADLNDEWVQR ALHFAISEYN KATKDDYYRR PLRVLRARQQ TVGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WENRRSLVKS RCQES.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Activated Leukocyte Cell Adhesion Molecule (CD166) Mouse Recombinant

Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

Product # :

PRO-2749

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

ALCAM mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 739 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa. ALCAM is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ALCAM protein solution (0.25mg/ml) contains 50% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to block the adhesion of Jurkat human acute T cell leukemia cells to immobilized Recombinant Human CD6. When cells are added to 1 ug/ml of mouse ALCAM binded to CD6, this effect is more to 50%.

More Info

Introduction
CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.
Synonyms
Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
WYTVNSAYGD TIVMPCRLDV PQNLMFGKWK YEKPDGSPVF IAFRSSTKKS VQYDDVPEYK DRLSLSENYT LSIANAKISD EKRFVCMLVT EDNVFEAPTL VKVFKQPSKP EIVNKAPFLE TDQLKKLGDC ISRDSYPDGN ITWYRNGKVL QPVEGEVAIL FKKEIDPGTQ LYTVTSSLEY KTTRSDIQMP FTCSVTYYGP SGQKTIYSEQ EIFDIYYPTE QVTIQVLPPK NAIKEGDNIT
LQCLGNGNPP PEEFMFYLPG QPEGIRSSNT YTLTDVRRNA TGDYKCSLID KRNMAASTTI TVHYLDLSLN PSGEVTKQIG DTLPVSCTIS ASRNATVVWM KDNIRLRSSP SFSSLHYQDA GNYVCETALQ EVEGLKKRES LTLIVEGKPQ IKMTKKTDPS GLSKTIICHV EGFPKPAIHW TITGSGSVIN QTEESPYING RYYSKIIISP EENVTLTCTA ENQLERTVNS LNVSAISIPE
HDEADDISDE NREKVNDQAK LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK HHHHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

APRIL Human Recombinant

Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.

Product # :

CYT-815

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page

Description

APRIL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (105-247) and having a molecular mass of 17.6kDa.APRIL is fused to a 16 amino acid T7-tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

APRIL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines.
Synonyms
Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.
Background
APRIL Human Recombinant: Expanding the Horizons of Immunotherapy
Abstract:

APRIL (A Proliferation-Inducing Ligand) is a promising molecule within the tumor necrosis factor (TNF) superfamily that plays a pivotal role in immune regulation. This research paper provides an overview of APRIL human recombinant, exploring its potential applications in immunotherapy. Understanding the mechanisms and therapeutic implications of APRIL holds promise in the field of immune-related disorders. This article presents a concise analysis of APRIL, highlighting its potential as a therapeutic target.
Introduction:

Immunotherapy has revolutionized the treatment of various diseases by harnessing the power of the immune system. APRIL, a member of the TNF superfamily, has emerged as a potential candidate for immunotherapeutic interventions. This paper provides an overview of APRIL, shedding light on its structure, function, and potential applications in immunotherapy.
APRIL Structure and Function:

APRIL is a transmembrane protein that can be proteolytically cleaved, leading to the generation of soluble forms. It interacts with its receptors, such as BCMA and TACI, to regulate immune responses. APRIL influences B-cell activation, proliferation, and antibody production, making it a compelling target for immunotherapeutic strategies.
Immunotherapeutic Applications of APRIL Human Recombinant:

APRIL human recombinant holds great potential in immunotherapy. By modulating APRIL activity, it may be possible to enhance immune responses against cancer cells or dampen immune dysregulation in autoimmune disorders. Additionally, APRIL-based therapeutics could be developed to target specific immune cell populations or enhance the efficacy of existing immunotherapies.
Challenges and Future Directions:

Although APRIL shows promise, there are challenges to overcome. Further research is needed to elucidate the precise mechanisms of APRIL-mediated immune regulation and identify optimal therapeutic approaches. Additionally, safety considerations and potential side effects must be thoroughly evaluated.
Conclusion:

APRIL human recombinant represents a valuable tool for advancing immunotherapy. Understanding the structure, function, and therapeutic potential of APRIL opens up new avenues for treating immune-related disorders. Continued research and development in this field have the potential to revolutionize the landscape of immunotherapy, improving patient outcomes and expanding the possibilities for personalized medicine.
What is the molecular weight/Mw of APRIL Protein?
APRIL Protein has a total Mw of 17.6kDa.

What is the source or expression system of APRIL Protein?
Escherichia Coli.

What is the Purity of APRIL Protein?
APRIL Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of APRIL Protein?
The biological functionality of APRIL Protein will be determined in the future.

What is the amino acid sequence of APRIL Protein?
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.

What applications can APRIL Protein be used in?
APRIL Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APRIL Protein?
The endotoxin level is minimal, APRIL Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

I-309 Human Recombinant (CCL1)

Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

Product # :

CHM-312

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

I-309 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8504 Dalton. The I-309 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CCL1 protein was lyophilized with no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

More Info

Introduction
Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.
Synonyms
Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized I-309 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized I-309 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Ser-Met-Gln.
Background
What is the molecular weight/Mw of CCL1 HUMAN Protein?
CCL1 HUMAN Protein has a total Mw of 8.5kDa.

What is the source or expression system of CCL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL1 HUMAN Protein?
CCL1 HUMAN Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL1 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Ser-Met-Gln.

What applications can CCL1 HUMAN Protein be used in?
CCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL1 HUMAN Protein?
The endotoxin level is minimal, CCL1 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Beta Defensin -1 Rat Recombinant

Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.

Product # :

CYT-062

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

BD-1 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4.1kDa.The BD-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BD-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

More Info

Introduction
The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
Beta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.
Synonyms
Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BD-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized BD-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.
Background
What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 4.1kDa.

What is the source or expression system of BD1 Protein?
Escherichia Coli.

What is the Purity of BD1 Protein?
BD1 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of BD1 Protein?
Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

What is the amino acid sequence of BD1 Protein?
DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Casein Kinase 2 beta Human Recombinant

PKCK2 Beta, PKCK2B, CK2N, CSK2B, MGC138222, MGC138224, G5A, Phosvitin, Casein Kinase 2 beta, Casein Kinase 2B, Casein Kinase 2 beta, Casein kinase 2 beta polypeptide, Casein kinase II subunit beta, CK II beta, CK2B, CSNK 2B, CSNK2B, G5A

Product # :

PKA-129

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CSNK2B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-215 a.a) and having a molecular mass of 24.9 kDa.CSNK2B is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CSNK2B protein solution (1mg/ml) in 0.2M NaCl, 20mM Tris-HCl buffer (pH 8.0), 1mM EDTA, 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Casein Kinase 2 beta (CSNK2B) is a ubiquitous Ser/Thr kinase expressed in all eukaryotes. CSNK2Bis atetramer comprised of 2 catalytic kinase domains, alpha subunits and 2 identical regulatory beta subunits.CSNK2Btakes part incell cycle control, DNA repair,regulation of the circadian rhythm and other cellularprocesses. The beta subunit itself confers stability to the CK2 alpha subunitand is involved in activity and substrate specificity but does not have kinase activity.
Synonyms
PKCK2 Beta, PKCK2B, CK2N, CSK2B, MGC138222, MGC138224, G5A, Phosvitin, Casein Kinase 2 beta, Casein Kinase 2B, Casein Kinase 2 beta, Casein kinase 2 beta polypeptide, Casein kinase II subunit beta, CK II beta, CK2B, CSNK 2B, CSNK2B, G5A
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-4 Human Recombinant

HBGF4, FGF-4, FGF4, KFGF, HSTF1.

Product # :

CYT-312

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. The FGF4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FGF4 protein was lyophilized with 20mM sodium phosphate and 500mM NaCl pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X10⁶ units/mg.

More Info

Introduction
FGF4 holds s comprehensive mitogenic and cell survival activities and takes part in a range of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF4 possess oncogenic transforming activity. FGF4 and FGF3, oncogenic growth factors are localized on chromosome 11. Co-amplification of both factors was found in several kinds of human tumors. FGF4 functions in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.
Synonyms
HBGF4, FGF-4, FGF4, KFGF, HSTF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-4 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGF4 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.
Background
What is the molecular weight/Mw of FGF4 HUMAN Protein?
FGF4 HUMAN Protein has a total Mw of 19.8kDa.

What is the source or expression system of FGF4 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF4 HUMAN Protein?
FGF4 HUMAN Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF4 HUMAN Protein?
The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.

What is the amino acid sequence of FGF4 HUMAN Protein?
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.

What applications can FGF4 HUMAN Protein be used in?
FGF4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF4 HUMAN Protein?
The endotoxin level is minimal, FGF4 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-acidic (154 a.a.) Human Recombinant

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Product # :

CYT-1112

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Fibroblast Growth Factor-acidic Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 17.3kDa. The FGF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4, with 0.5mM DTT, 2mM EDTA, and 5 % Trehalose.

Purity

Greater than 97.0% as determined by:

(a) Analysis by RP-HPLC.

(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×10⁶IU/mg in the presence of 10µg/ml Heparin.

More Info

Introduction
Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF1 functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor.FGF1 acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-acidic should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-acidic Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF 1 Protein?
Escherichia Coli.

What is the Purity of FGF 1 Protein?
FGF 1 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×106 IU/mg in the presence of 10µg/ml Heparin.

What is the amino acid sequence of FGF 1 Protein?
AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.

What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Beta-Nerve Growth Factor Mouse

Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

Product # :

CYT-440

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

NGF beta Mouse produced in Submaxillary Gland of Grown Mouse is a homodimer, non-glycosylated, polypeptide chain containing 2 identical 120 amino acids and having a molecular mass of 13,471 Dalton each.The NGF beta Mouse is purified by advanced biology purification technology.

Source

Submaxillary Gland of Grown Mouse.

Formulation

The NGF beta Mouse was lyophilized from solution containing 5% mannitol and 1% HSA.

Purity

Greater than 98% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE .

Biological Activity

The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

More Info

Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse Beta-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Murine NGF-Beta should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Murine NGF-beta in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.
Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 13kDa.

What is the source or expression system of B NGF Protein?
Submaxillary Gland of Grown Mouse.

What is the Purity of B NGF Protein?
B NGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of B NGF Protein?
The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

What is the amino acid sequence of B NGF Protein?
SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.

What applications can B NGF Protein be used in?
B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for XXX Protein?
The endotoxin level is minimal, XXX Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

WNT Inhibitory Factor 1 Mouse Recombinant

Wnt inhibitory factor 1, WIF-1, Wif1.

Product # :

PRO-2248

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

WIF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 359 amino acids (29-379a.a.) and having a molecular mass of 39.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).WIF1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

WIF1 protein solution (1mg/ml) contains 20mM MES (pH5.5), 1mM DTT, 1mM PMSF and 30% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.
Synonyms
Wnt inhibitory factor 1, WIF-1, Wif1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
GQPPEESLYL WIDAHQARVL IGFEEDILIV SEGKMAPFTH DFRKAQQRMP AIPVNIHSMN FTWQAAGQAE YFYEFLSLRS LDKGIMADPT VNVPLLGTVP HKASVVQVGF PCLGKQDGVA AFEVNVIVMN SEGNTILRTP QNAIFFKTCQ QAECPGGCRN GGFCNERRVC ECPDGFYGPH
CEKALCIPRC MNGGLCVTPG FCICPPGFYG VNCDKANCST TCFNGGTCFY PGKCICPPGL EGEQCELSKC PQPCRNGGKC IGKSKCKCPK GYQGDLCSKP VCEPGCGAHG TCHEPNKCQC REGWHGRHCN KRYGASLMHA PRPAGAGLER HTPSLKKAED RRDPPESNYI WVEHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Coronavirus 2019 Nucleocapsid (196 a.a.), Recombinant

Product # :

SARS-042

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

The E.Coli derived recombinant protein contains the Coronavirus 2019 middle region a.a. from the Nucleocapsid protein and fused to GST-6xHis tag at N-terminal and having a Mw. Of 48.4 kDa.

Source

E.Coli.

Formulation

CoV-2 Nucleocapsid protein solution is supplied in 50mM Tris-HCl pH 8, 1M Urea, and 50% Glycerol.

Purity

CoV-2 Nucleocapsid protein is >95% pure as determined SDS-PAGE.

More Info

Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
Physical Appearance
Sterile Filtered clear solution.
Stability
CoV-2 Spike Protein is shipped on ice packs. Upon arrival, Store at -20°C.
Purification Method
NTA Sepharose-Affinity Purification.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor (Leu-21) Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-466

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.The EGF 21-Leu is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

More Info

Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.
Background
Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications
Abstract:
This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications.
Introduction:
Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance.
Molecular Insights and Signaling Dynamics:
The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis.
Experimental Profiling and Cellular Responses:
In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Prospects:
Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions.
Future Challenges and Prospects:
While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21).
Conclusion:
In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.

What is the source or expression system of EGF Protein?
Escherichia Coli.

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.

What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Farnesyl-Diphosphate Farnesyltransferase 1 Human Recombinant

Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.

Product # :

ENZ-820

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

FDFT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-283 a.a) and having a molecular mass of 35.4 kDa. FDFT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FDFT1 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Farnesyl-Diphosphate Farnesyltransferase 1, also known as FDFT1 is a membrane-associated enzyme sited at a branch point in the mevalonate pathway. FDFT1belongs to the phytoene/squalene synthase family. FDFT1 is the 1st specific enzyme in cholesterol biosynthesis, which catalyzes the dimerization of 2 molecules of farnesyl diphosphate in a two-step reaction to form squalene.
Synonyms
Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEFVKCL GHPEEFYNLV RFRIGGKRKV MPKMDQDSLS SSLKTCYKYL NQTSRSFAAV IQALDGEMRN AVCIFYLVLR ALDTLEDDMT ISVEKKVPLL HNFHSFLYQP DWRFMESKEK DRQVLEDFPT ISLEFRNLAE KYQTVIADIC RRMGIGMAEF LDKHVTSEQE WDKYCHYVAG LVGIGLSRLF SASEFEDPLV GEDTERANSM GLFLQKTNII RDYLEDQQGG REFWPQEVWS RYVKKLGDFA KPENIDLAVQ CLNELITNAL HHIPDVITYL SRLRNQ.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Placental Growth Factor-1 Mouse Recombinant

Placenta growth factor, PlGF, PGF1.

Product # :

CYT-907

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

PGF1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 138 amino acids (27-158a.a.) and having a molecular mass of 15.9kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). PGF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

PGF1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 0.1mM PMSF and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Placental Growth Factor, also known as PGF is rich in trophoblastic giant cells which are linked with the parietal yolk sac at early stages of embryogenesis. Furthermore, the secretion of PGF by trophoblastic giant cells is the signal which initiates as well as co-ordinates vascularization in the deciduum and placenta during early embryogenesis.
Synonyms
Placenta growth factor, PlGF, PGF1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
AGNNSTEVEV VPFNEVWGRS YCRPMEKLVY ILDEYPDEVS HIFSPSCVLL SRCSGCCGDE GLHCVPIKTA NITMQILKIP PNRDPHFYVE MTFSQDVLCE CRPILETTKA ERRKTKGKRK RSRNSQTEEP HPHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Desert Hedgehog (C23II) Human Recombinant

HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

Product # :

CYT-362

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

DHH (C23II) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 19.9kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The Biological Activity was determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED₅₀ for this effect is 15-45 μg/ml.

More Info

Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.
Synonyms
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IIGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

soluble CD40 Ligand/TRAP Human Recombinant, His Tag

CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L, CD40LG.

Product # :

CYT-670

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CD40LG Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 169 amino acids (113-261 a.a.) and having a molecular mass of 18.3kDa. The CD40LG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CD40LG solution (0.5mg/ml) 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.2M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
CD40L or CD154 is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines. CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes. It also costimulates proliferation of activated T-cells and this is accompanied by the production of IFN-gamma , TNF-alpha , and IL2.
Synonyms
CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L, CD40LG.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQKGDQNPQI AAHVISEASS KTTSVLQWAE KGYYTMSNNL VTLENGKQLT VKRQGLYYIY AQVTFCSNRE ASSQAPFIAS LCLKSPGRFE RILLRAANTH SSAKPCGQQS IHLGGVFELQ PGASVFVNVT DPSQVSHGTG FTSFGLLKL.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Calnueron-1 Human Recombinant

Calcium-binding protein 8, CaBP8, Calneuron I, Calneuron-1, CALN1, CABP8.

Product # :

PRO-279

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CALN1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 24kDa. The CALN1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CALN1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 50mM NaCl and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
CALN1 is highly similar to the calcium-binding proteins of the calmodulin family. The CALN1 protein contains two EF-hand domains and potential calcium-binding sites. Also, CALN1 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. CALN1 has a role in the physiology of neurons and is potentially significant in memory and learning.
Synonyms
Calcium-binding protein 8, CaBP8, Calneuron I, Calneuron-1, CALN1, CABP8.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPFHHVTAGL LYKGNYLNRS LSAGSDSEQL ANISVEELDE IREAFRVLDR DGNGFISKQE LGMAMRSLGY MPSEVELAII MQRLDMDGDG QVDFDEFMTI LGPKLVSSEG RDGFLGNTID SIFWQFDMQR ITLEELKHIL YHAFRDHLTM KDIENIIINE EESLNETSGN CQTEFEGVHS QKQNRQTCVR KS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cytomegalo Virus gB Recombinant

Product # :

CMV-211

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

The E.Coli derived recombinant artificial mosaic protein contains the CMV gB immunodominant regions 11-67 amino acids, fused with a 26 kDa GST Tag, the protein weight is 6.5kDa, having a total weight of 32.5 kDa.

Source

Escherichia Coli.

Formulation

50mM Tris pH 7.2, 1mM EDTA and 50% glycerol.

Purity

CMV gB protein is >95% pure as determined by 10% PAGE (coomassie staining).

More Info

Introduction
MV belongs to the Beta herpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods.CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.
Stability
CMV gB protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Specificity
Immunoreactive with sera of CMV-infected individuals.
Purification Method
CMV gB was purified by proprietary chromatographic technique.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Endoglin Human Recombinant, Sf9

CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

Product # :

CYT-389

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.

Source

Sf9 Insect Cells.

Formulation

Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

More Info

Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 90kDa.

What is the source or expression system of CD105 Protein?
Sf9 Insect Cells.

What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CD105 Protein?
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

What is the amino acid sequence of CD105 Protein?
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

DnaJ (Hsp40) Homolog, Subfamily C, Member 12 Human Recombinant

DnaJ homolog subfamily C member 12, J domain-containing protein 1, DNAJC12, JDP1, RP11-57G10.2.

Product # :

HSP-053

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

DNAJC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (1-198) and having a molecular mass of 26kDa (Molecular weight on SDS-PAGE will appear higher).DNAJC12 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The DNAJC12 solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 2mM DTT and 100mM NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
DnaJ (Hsp40) Homolog, Subfamily C, Member 12 (DNAJC12) belongs to the DnaJ/Hsp40 family. DnaJ/Hsp40 family members are linked with complex assembly, protein folding, and export. DnaJ/Hsp40 proteins are extremely conserved throughout evolution and function as co-chaperones regulating protein folding, transport, translational initiation and gene expression. DnaJC12 has a role in protein folding and export and is believed to be involved in estrogen control and the development of breast cancer. DNAJC12 is expressed at high levels in the brain, heart, and testis, and at reduced levels in the kidney and stomach.
Synonyms
DnaJ homolog subfamily C member 12, J domain-containing protein 1, DNAJC12, JDP1, RP11-57G10.2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMDAILN YRSEDTEDYY TLLGCDELSS VEQILAEFKV RALECHPDKH PENPKAVETF QKLQKAKEIL TNEESRARYD HWRRSQMSMP FQQWEALNDS VKTSMHWVVR GKKDLMLEES DKTHTTKMEN EECNEQRERK KEELASTAEK TEQKEPKPLE KSVSPQNSDS SGFADVNGWH LRFRWSKDAP SELLRKFRNY EI.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

sds-page

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity