Search: 1000 results found for "Growth Hormone"

Description:

Adiponectin Human Recombinant, Trimeric form

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-233

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Description

Trimeric form of Adiponectin Human trimeric form was expressed in HEK293 cells. The cysteine 39 was replaced with Alanine (C39A) 9. hAd-C39A can only form a trimer, but not a hexamer or an HMW form.

Source

HEK293 (Human embryonic kidney cell line).

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl, pH 7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.

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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue.
Many studies demonstrate that Adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle. Attenuate hepatic lipogenesis and gluconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, Adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of Adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Adiponectin 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
Add deionized water to a working volume of 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 in the cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25 kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293.

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

What is the Biological Activity of ADIPONECTIN Protein?
ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.
What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.

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

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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:

HSA Human Protein

HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

Product # :

PRO-354

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Description

HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.

Source

Human Serum.

Formulation

0.2gr/ml solution containing no additives.

Purity

Greater than 97.0% as determined by SDS-PAGE.

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Introduction
HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications.
Synonyms
HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Physical Appearance
Sterile Filtered clear yellowish solution.
Stability
HSA although stable at room temperature for 2 weeks should be stored at 4°C.

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:

IFN-Gamma Mouse Recombinant

Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-358

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Description

IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
Background
What is the molecular weight/Mw of IFNG MOUSE Protein?
IFNG MOUSE Protein has a total Mw of 15.6kDa.

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

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

What is the Biological Activity of IFNG MOUSE Protein?
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg

What is the amino acid sequence of IFNG MOUSE Protein?
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.

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

What is the endotoxin level for IFNG MOUSE Protein?
The endotoxin level is minimal, IFNG 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:

Pleckstrin homology-like domain family A member 2 Human Recombinant

Pleckstrin homology-like domain family A member 2, Imprinted in placenta and liver protein, Tumor-suppressing subchromosomal transferable fragment candidate gene 3 protein, Tumor-suppressing STF cDNA 3 protein, Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene C protein, p17-Beckwith-Wiedemann region 1 C, PHLDA2, BWR1C, HLDA2, IPL, TSSC3, BRW1C.

Product # :

PRO-781

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Description

PHLDA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids (1-152 a.a.) and having a molecular mass of 19.2 kDa. PHLDA2 is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PHLDA2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Pleckstrin homology-like domain family A member 2 (PHLDA2) is a cytoplasmic protein, which is involved in fetal and placental growth. PHLDA2 is an apoptosis-related protein, which acts as a negative growth regulator and is expressed during normal human development. PHLDA2 is imprinted on placenta, liver and fetal tissues during embryogenesis and is removed once development is complete. The PHLDA2 gene is one of a number of genes in the imprinted gene domain of 11p15.5 which is considered to be an important tumor suppressor gene region. Changes in this region may be linked to the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. PHLDA2 is expressed in placenta (present in all cells of the villous cytotrophoblast) and adult prostate gland. Furthermore, PHLDA2 is expressed in adult brain and neuroblastoma, medullablastoma and glioblastoma cell lines and at low levels in adult liver and lung, and fetal liver.
Synonyms
Pleckstrin homology-like domain family A member 2, Imprinted in placenta and liver protein, Tumor-suppressing subchromosomal transferable fragment candidate gene 3 protein, Tumor-suppressing STF cDNA 3 protein, Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene C protein, p17-Beckwith-Wiedemann region 1 C, PHLDA2, BWR1C, HLDA2, IPL, TSSC3, BRW1C.
Physical Appearance
Sterile filtered colorless solution.
Stability
PHLDA2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKSPDEVLRE GELEKRSDSL FQLWKKKRGV LTSDRLSLFP ASPRARPKEL RFHSILKVDC VERTGKYVYF TIVTTDHKEI DFRCAGESCW NAAIALALID FQNRRALQDF RSRQERTAPA APAEDAVAAA AAAPSEPSEP SRPSPQPKPR TP.

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 Mouse Recombinant, Biotin

Urogastrone, URG, EGF.

Product # :

CYT-841

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Description

EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.

Source

Escherichia Coli.

Formulation

The protein (0.5mg/ml) solution contains sterile PBS.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x10⁶units/mg.

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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 clear solution.
Stability
Should be stored at 4°C.Please do not freeze.
Amino Acid Sequence
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
Background
Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential
Abstract:
This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.
Introduction:
Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.
Protein Engineering and Biotin Conjugation:
EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.
Cellular Signaling Amplification:
The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.
Cellular Assays and Functional Responses:
In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.
Tailored Delivery Strategies:
The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.
Regenerative Medicine and Targeted Therapy:
The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.
Future Prospects and Challenges:
While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.
Conclusion:
In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.
What is the molecular weight/Mw of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein has a total Mw of 7kDa.

What is the source or expression system of MEGF, BIOTIN Protein?
Escherichia Coli.

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

What is the Biological Activity of MEGF, BIOTIN Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

What is the amino acid sequence of MEGF, BIOTIN Protein?
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

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

What is the endotoxin level for MEGF, BIOTIN Protein?
The endotoxin level is minimal, MEGF, BIOTIN 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:

Tumor Type M2 Pyruvate Kinase Human Recombinant

Pyruvate kinase isozymes M1/M2, EC 2.7.1.40, Pyruvate kinase muscle isozyme, Pyruvate kinase 2/3, Cytosolic thyroid hormone-binding protein, CTHBP, THBP1, M2PK, PKM2, PK3, PK2, PKM, TCB, OIP3, MGC3932, Tumor Type M2 Pyruvate Kinase.

Product # :

PKA-339

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Description

PKM2 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 551 amino acids (1-531 a.a.) and having a molecular mass of 60.1kDa. The PKM2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PKM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The Specific activity is > 25,000 pmol/min/ug. 1 unit will form 1pmol of phospho(enol)pyruvate to pyruvate per minute at pH 7.5 at 37°C.

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Introduction
Pyruvate kinase is a key enzyme in the glycolytic pathway. The M2 isoenzyme of pyruvate kinase is specifically expressed at high levels in tumor cells, and can be measured in plasma of patients with advanced breast cancer. The marker is useful for measuring disease activity, sensitivity to chemotherapy and recurrence.
Synonyms
Pyruvate kinase isozymes M1/M2, EC 2.7.1.40, Pyruvate kinase muscle isozyme, Pyruvate kinase 2/3, Cytosolic thyroid hormone-binding protein, CTHBP, THBP1, M2PK, PKM2, PK3, PK2, PKM, TCB, OIP3, MGC3932, Tumor Type M2 Pyruvate Kinase.
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 MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE ATAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P.

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:

Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag

Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8

Product # :

CHM-047

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Description

Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
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.
Applications
Immunoassay.
Background
What is the source or expression system of CXCL8 HUMAN, GST Protein?
Escherichia Coli.

What is the Purity of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 HUMAN, GST Protein?
The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.

What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is composed from 72 amino acids.

What applications can CXCL8 HUMAN, GST Protein be used in?
CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 HUMAN, GST Protein?
The endotoxin level is minimal, CXCL8 HUMAN, GST 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:

Glutamate Decarboxylase 2 Human Recombinant

Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kDa), Glutamate Decarboxylase 65 KDa Isoform, 65 KDa Glutamic Acid Decarboxylase, EC 4.1.1.15, GAD-65, GAD65, Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kD), Glutamate Decarboxylase-2 (Pancreas), EC 4.1.1, GAD2.

Product # :

ENZ-937

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Description

Recombinant Human GAD2 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 61 kDa. GAD2 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

GAD2 protein solution is supplied in 20mM Sodium phosphate pH-7.4, 150mM NaCl, 0.016mM Pyridoxal-5’-Phosphate, 0.05% Tergitol 15-S-9 and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Glutamate Decarboxylase 2 (GAD2) is one of several forms of glutamic acid decarboxylase, identified as a main autoantigen in type II diabetes. The GAD2 enzyme is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for the GAD2 enzyme has been characterized in the human pancreas since it has been identified as an autoantibody and an autoreactive T cell target in type II diabetes. GAD2 gene may also have a role in the stiff man syndrome. In addition, GAD2 catalyzes the production of GABA.
Synonyms
Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kDa), Glutamate Decarboxylase 65 KDa Isoform, 65 KDa Glutamic Acid Decarboxylase, EC 4.1.1.15, GAD-65, GAD65, Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kD), Glutamate Decarboxylase-2 (Pancreas), EC 4.1.1, GAD2.
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. Avoid multiple freeze-thaw cycles.

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:

Interleukin 10 Human Recombinant, Sf9, Active

Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.

Product # :

CYT-1147

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Description

IL-10 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 166 amino acids (19-178 aa) and having a molecular mass of 19.4kDa. IL-10 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL-10 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using MC/9 mouse mast cells. The ED50 range < 5 ng/ml.

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Introduction
Interleukin 10 or IL-10 or human cytokine synthesis inhibitory factor, is a cytokine (anti-inflammatory). IL10 gene is coding for il-10 In humans. Interleukin 10 has a receptor complex that is built from a couple of IL-10 receptor-1 and a couple of IL-10 receptor-2 proteins. therfore, the whole receptor unit consists of four IL-10 receptor molecules. IL-10 binds the receptor and causes STAT3 signalling through the phosphorylation of the cytoplasmic ends of IL-10 receptor 1 and IL-10 receptor 2 through JAK1 and Tyk2.
Synonyms
Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.
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
SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN 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:

Crystallin Alpha A Human Recombinant

CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-4.

Product # :

HSP-002

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Description

Recombinant Human CRYAA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids and having a molecular mass of 19.9kDa.CRYAA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CRYAA protein contains 20mM Tris-HCl buffer (pH 7.5), 50mM NaCl and 1mM EDTA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein(sHSP also known as the HSP20). They act as molecular chaperones and hold them in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. The expression of alpha-A is preferentially restricted to the lens cell.
Synonyms
CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-4.
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
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSGISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRLPSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS.

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:

Activin A Receptor Type II-Like 1 Human Recombinant

Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.

Product # :

CYT-920

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Description

ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (22-118a.a.) and having a molecular mass of 11.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

ACVRL1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
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
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
Background
The Physiological Implications and Therapeutic Potential of Activin A Receptor Type II-Like 1 Human Recombinant
1. Abstract
This research paper investigates the Activin A Receptor Type II-Like 1 Human Recombinant (ACVRL1), a significant protein involved in the TGF-beta superfamily signaling pathway. We provide an extensive understanding of ACVRL1’s structure, signaling mechanism, biological functions, and implications in disease pathology. Additionally, we explore the therapeutic potential of ACVRL1 in various pathological conditions.
2. Introduction
ACVRL1, also known as ALK1, plays an essential role in the TGF-beta signaling pathway, which has implications in cellular proliferation, differentiation, and apoptosis. Understanding ACVRL1 and its signaling mechanisms could provide insights into its potential therapeutic applications in various diseases.
3. Structure and Signaling of ACVRL1
ACVRL1 is a type I receptor protein involved in the TGF-beta signaling pathway. It is a transmembrane protein that consists of a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Binding of ligands to ACVRL1 triggers phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVRL1
ACVRL1 plays pivotal roles in multiple biological processes, including vascular development, angiogenesis, and maintenance of vascular integrity. It is known to influence cellular processes such as proliferation, differentiation, and apoptosis, thereby implicating it in organogenesis and homeostasis.
5. ACVRL1 in Disease Pathology
Mutations in the ACVRL1 gene have been associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation. This link underscores the critical role of ACVRL1 in vascular biology and disease.
6. Therapeutic Potential of ACVRL1
Given its crucial role in vascular biology and its link to HHT, ACVRL1 presents a promising target for therapeutic interventions. Modulation of ACVRL1 signaling could potentially provide treatment options for pathological conditions related to abnormal blood vessel formation and function.
7. Conclusion and Future Perspectives
Our understanding of ACVRL1 and its functions has grown significantly in recent years, but there is much yet to be discovered. Continued research into ACVRL1's precise molecular mechanisms and its roles in disease will undoubtedly open new doors for therapeutic developmen
What is the molecular weight / Mw of ACVRL1 Protein?
ACVRL1 Protein has a total Mw of 11.5kDa.
What is the source or expression system of ACVRL1 Protein?
Sf9, Insect cells.

What is the Purity of ACVRL1 Protein?
ACVRL1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of ACVRL1 Protein?
The biological functionality of ACVRL1 Protein will be determined in the future.

What is the amino acid sequence of ACVRL1 Protein?
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.

What applications can ACVRL1 Protein be used in?
ACVRL1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ACVRL1 Protein?
The endotoxin level is minimal, ACVRL1 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:

Leptin Antagonist Triple Mutant Pegylated Rat Recombinant

Product # :

CYT-567

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Description

Leptin Antagonist Triple Mutant Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Rat Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Rat Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Leptin Antagonist Triple Mutant Rat Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Rat Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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:

Galectin-2, BioActive Mouse Recombinant

Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.

Product # :

CYT-1155

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Description

LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.

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Introduction
Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.
Synonyms
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE
Background
What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.

What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
Escherichia Coli.

What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.

What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.

What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE 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:

Syntaphilin Human Recombinant

KIAA0374, MGC46096, bA314N13.5, SNPH, Syntaphilin.

Product # :

PRO-545

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Description

SNPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 444 amino acids (1-424) and having a molecular mass of 48.2 kDa.The SNPH is fused to 20 amino acid His-Tag at N-terminus and purified by standard chromatography techniques.

Source

Escherichia Coli.

Formulation

The Syntaphilin protein solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Syntaxin-1, synaptobrevin, and SNAP25 cooperate to form the SNARE complex, which is needed for synaptic vesicle docking and fusion SNPH is a neuron-specific protein originally characterized as a binding partner of syntaxin-1. SNPH participates with SNAP25 for the binding to Syntaxin-1 and prevents the construction of the SNARE core complex, thus manageling free syntaxin-1 availability for the assembly of the SNARE complex and potentially regulating synaptic vesicle exocytosis. Expression Syntaphilin appears to be brain-specific. SNPH is an inhibitor of both SNARE-based fusion and dynamin-mediated endocytosis.
Synonyms
KIAA0374, MGC46096, bA314N13.5, SNPH, Syntaphilin.
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 MAMSLPGSRR TSAGSRRRTS PPVSVRDAYG TSSLSSSSNS GSYKGSDSSP TPRRSMKYTL CSDNHGIKPPTPEQYLTPLQ QKEVCIRHLK ARLKDTQDRL QDRDTEIDDL KTQLSRMQED WIEEECHRVE AQLALKEARK EIKQLKQVID TVKNNLIDKDKGLQKYFVDI NIQNKKLETL LHSMEVAQNG MAKEDGTGES AGGSPARSLT RSSTYTKLSD PAVCGDRQPG DPSSGSAEDG ADSGFAAADD
TLSRTDALEA SSLLSSGVDC GTEETSLHSS FGLGPRFPAS NTYEKLLCGM EAGVQASCMQ ERAIQTDFVQ YQPDLDTILE KVTQAQVCGTDPESGDRCPE LDAHPSGPRD PNSAVVVTVG DELEAPEPIT RGPTPQRPGA NPNPGQSVSV VCPMEEEEEA AVAEKEPKSY WSRH.

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:

Transforming Growth Factor-Beta 1 Rat Recombinant

Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.

Product # :

CYT-1265

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Quantity :

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Shipped at Room temp

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Description

Transforming Growth Factor-Beta 1 Rat Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa.
TGFB1 Rat Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

The biological activity was determined by TGFB1 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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Synonyms
Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 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 Transforming Growth Factor-Beta 1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSALDTNYC FSSTEKNCCV RQLYIDFRKD LGWKWIHEPK GYHANFCLGP CPYIWSLDTQ YSKVLALYNQ HNPGASASPC CVPQALEPLP IVYYVGRKPK VEQLSNMIVR SCKCS.
Background
Mouse TGF-β1 as an inducer of EMT [epithelial–mesenchymal transition ] therefore used in in fibrosis, wound healing, cancer invasion, and metastasis. Mouse TGF-β1 decreases E-cadherin expression and increases N-cadherin, vimentin and fibronectin.
TGF-β1 is produced by T regulatory cells (Tregs), Macrophages and monocytes, Platelets, Fibroblasts, Epithelial cells, Endothelial cells, Smooth muscle cells, Tumor cells, Activated immune cells
What is the source or expression system of Mouse TGFB1 Protein?
CHO Cells

What is the Purity of Mouse TGFB1 Protein?
Mouse TGFB1 Protein is >97% pure as determined by SDS-PAGE and SEC-HPLC analyses.

What is the molecular weight of Mouse TGFB1 Protein?
Mouse TGFB1 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Mouse TGFB1 Protein?
The biological functionality of Mouse TGFB1 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Mouse TGFB1 Protein?
The endotoxin level is minimal, Mouse TGFB1 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Mouse TGFB1 Protein?
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASASPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.

Is TGFB1 a homodimer / homodimeric protein?
Yes, TGFB1 is homo dimer consisting of 2 identical chains.

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:

Precursor Brain-Derived Neurotrophic Factor Human Recombinant

proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

Product # :

CYT-014

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

proBDNF Human Recombinant produced in E.Coli is a single, non-glycosylated, non-covalently linked homodimer with each polypeptide chain containing 229 amino acids and having a molecular mass of 52kDa. The proBDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

proBDNF was lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH 8.0 and 500mM NaCl.

Purity

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

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Introduction
proBDNF (the precursor form of Brain-derived neurotrophic factor) interacts preferentially with p75NTR (the pan-neurotrophin receptor p75) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, while the mature BDNF selectively binds with great affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. Since proneurotrophins and mature neurotrophins bring forth opposite biological effects, proBDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. proBDNF has an important role in negative regulation of neurotrophic actions in the brain.
Synonyms
proBDNF, Precursor Form Brain-derived Neurotrophic Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized proBDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution proBDNF 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 proBDNF in sterile 18M-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 Met-Ala-Pro-Met-Lys.
Background
Precursor Brain-Derived Neurotrophic Factor Human Recombinant: Unveiling the Potential of a Key Neurotrophic Factor
Abstract:
Precursor Brain-Derived Neurotrophic Factor (proBDNF) human recombinant is a pivotal neurotrophic factor that plays a critical role in neuronal development, survival, and synaptic plasticity. This research paper provides a comprehensive overview of proBDNF, including its characteristics, processing mechanisms, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of proBDNF human recombinant are proposed, highlighting its future implications in the field of neuroregenerative medicine.
Introduction:
Understanding the intricate processes underlying neuronal development and function is crucial for advancing neuroregenerative strategies. Neurotrophic factors, such as proBDNF, have garnered significant attention due to their pivotal roles in supporting neuronal growth and survival. This paper delves into the unique features of proBDNF and presents novel approaches for its production and optimization.
Characteristics and Processing Mechanisms:
proBDNF is a precursor protein consisting of 247 amino acids and is processed into mature brain-derived neurotrophic factor (mBDNF) through proteolytic cleavage. The ratio between proBDNF and mBDNF is tightly regulated and determines the balance between neuronal survival and apoptosis. Additionally, proBDNF exerts distinct biological functions through its receptor interactions, modulating synaptic plasticity and neuronal activity.
Production of proBDNF Human Recombinant:
Efficient production methodologies are essential to harness the therapeutic potential of proBDNF human recombinant. Various expression systems, including bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents unique advantages and challenges, necessitating careful selection to achieve high yields and protein quality. Optimization strategies, such as codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality proBDNF recombinant.
Potential Therapeutic Applications:
proBDNF human recombinant holds immense promise for neuroregenerative medicine. Its role in promoting neuronal survival, axonal growth, and synaptic plasticity positions it as a valuable therapeutic agent for neurodegenerative disorders, spinal cord injuries, and stroke. Additionally, the balance between proBDNF and mBDNF presents a potential therapeutic target for fine-tuning neuronal processes and restoring proper brain function.
Conclusion:
proBDNF human recombinant represents a crucial neurotrophic factor with diverse therapeutic applications in neuroregenerative medicine. Optimizing production methodologies and further understanding its processing mechanisms will enhance its clinical utility. With its potential implications in neurodegenerative disorders and neuronal repair, proBDNF human recombinant holds immense promise as a transformative tool for promoting neural health and regeneration.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 52kDa.

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

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

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

What is the amino acid sequence of BDNF Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.

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

What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF 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:

Major Histocompatibility Complex Class I F Human Recombinant

CDA12, HLA-5.4, HLA-CDA12, HLAF, HLA class I histocompatibility antigen, alpha chain F, HLA F antigen, Leukocyte antigen F, MHC class I antigen F, HLA-F.

Product # :

PRO-2001

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Description

HLA-F Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (22-305a.a) and having a molecular mass of 35.1kDa. HLA-F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HLA-F protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Major Histocompatibility Complex Class I F (HLA-F) belongs to the MHC family which takes part in the presentation of antigens to the T cell receptor. HLA-F is a member of the class I molecules which are expressed in virtually all cells. There are 2 classes of HLA antigens. Class I molecules takes an important part in the immune system by presenting peptides derived from the endoplasmic reticulum.
Synonyms
CDA12, HLA-5.4, HLA-CDA12, HLAF, HLA class I histocompatibility antigen, alpha chain F, HLA F antigen, Leukocyte antigen F, MHC class I antigen F, HLA-F.
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 MGSGSHSLRY FSTAVSRPGR GEPRYIAVEY VDDTQFLRFD SDAAIPRMEP REPWVEQEGP QYWEWTTGYA KANAQTDRVA LRNLLRRYNQ SEAGSHTLQG MNGCDMGPDG RLLRGYHQHA YDGKDYISLN EDLRSWTAAD TVAQITQRFY EAEEYAEEFR TYLEGECLEL LRRYLENGKE TLQRADPPKA HVAHHPISDH EATLRCWALG FYPAEITLTW QRDGEEQTQD TELVETRPAG DGTFQKWAAV VVPPGEEQRY TCHVQHEGLP QPLILRWEQS PQPTIPI.

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:

Vascular Endothelial Growth Factor Receptor-1 Human Recombinant

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-240

Price :

Quantity :

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Description

Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

FLT1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity of FLT1 was determined by its ability to inhibit the VEGF (165)-induced proliferation of HUVECs.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH

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:

Major Histocompatibility Complex Class II DO Beta Human Recombinant

HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.

Product # :

PRO-1967

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Description

HLA-DOB Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (27-224) and having a molecular mass of 25.2 kDa.HLA-DOB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The HLA-DOB solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Major Histocompatibility Complex Class II DO Beta (HLA-DOB) is a part of the HLA class II beta chain paralogues. This class II beta chain is a heterodimer which is located in intracellular vesicles and consists of an alpha (DOA) and a beta chain (DOB), both anchored in the membrane. HLA-DOB which interacts with the HLA-DM molecule in B-cells is a significant modulator in the HLA class II restricted antigen presentation pathway. Class II molecules are expressed in antigen presenting cells such as B lymphocytes, dendritic cells and macrophages.
Synonyms
HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.
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 MGSGTDSPED FVIQAKADCY FTNGTEKVQF VVRFIFNLEE YVRFDSDVGM FVALTKLGQP DAEQWNSRLD LLERSRQAVD GVCRHNYRLG APFTVGRKVQ PEVTVYPERT PLLHQHNLLH CSVTGFYPGD IKIKWFLNGQ EERAGVMSTG PIRNGDWTFQ TVVMLEMTPE LGHVYTCLVD HSSLLSPVSV EWRAQSEYSW RK.

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:

High-Mobility Group Box 2 Human Recombinant

High mobility group (nonhistone chromosomal) protein B2, h mobility group box 2, HMG2.

Product # :

PRO-888

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Description

HMGB2 Human Recombinant produced in Baculovirus is a single polypeptide chain containing 232 amino acids (1-209) and having a molecular mass of 26.4 kDa.The HMGB2 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

The HMGB2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 30% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
HMGB2 belongs to the non-histone chromosomal high-mobility group protein family which are chromatin-associated and highly spread in the nucleus of higher eukaryotic cells. HMGB2 can successfully bend DNA and form DNA circles which indicates that HMGB2 facilitates cooperative interactions between cis-acting proteins by promoting DNA flexibility. Additionally, HMGB2 takes part in the final ligation step in DNA end-joining processes of DNA double-strand breaks repair and V(D)J recombination.
Synonyms
High mobility group (nonhistone chromosomal) protein B2, h mobility group box 2, HMG2.
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 TGSMGKGDPN KPRGKMSSYA FFVQTCREEH KKKHPDSSVN FAEFSKKCSE RWKTMSAKEK SKFEDMAKSD KARYDREMKN YVPPKGDKKG KKKDPNAPKR PPSAFFLFCS EHRPKIKSEH PGLSIGDTAK KLGEMWSEQS AKDKQPYEQK AAKLKEKYEK DIAAYRAKGK SEAGKKGPGR PTGSKKKNEP EDEEEEEEEE DEDEEEEDED EE.

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:

SH3 Domain Binding Glutamic Acid-Rich Protein Like Human Recombinant

SH3 domain-binding glutamic acid-rich-like protein, SH3BGRL, SH3BGR.

Product # :

PRO-1159

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Description

SH3BGRL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-114 a.a) and having a molecular mass of 15.3kDa.SH3BGRL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SH3BGRL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
SH3 domain-binding glutamic acid-rich-like protein (SH3BGRL) belongs to the human SH3BGR family. SH3BGRL gene which is located to chromosome Xq13.3, encodes a small protein of 114 amino acids that is extensively expressed in various tissues including liver and blood. SH3BGRL protein contains a prolinerich sequence (PLPPQIF), which is comprsed of both the SH3 binding (PXXP)3 and the Homer EVH1 binding (PPXXF)4 motif.
Synonyms
SH3 domain-binding glutamic acid-rich-like protein, SH3BGRL, SH3BGR.
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 MGSHMVIRVY IASSSGSTAI KKKQQDVLGF LEANKIGFEE KDIAANEENR KWMRENVPEN SRPATGYPLP PQIFNESQYR GDYDAFFEAR ENNAVYAFLG LTAPPGSKEA EVQAKQQA.

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:

SH3 Domain Binding Glutamic Acid-Rich Protein Like 3 Human Recombinant

SH3 Domain Binding Glutamic Acid-Rich Protein Like 3, SH3BGRL3-Like Protein, SH3 Domain-Binding Protein 1, SH3BP-1, TNF Inhibitory Protein, TIP-B1.

Product # :

PRO-1216

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Description

SH3BGRL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 116 amino acids (1-93) and having a molecular mass of 12.8 kDa.SH3BGRL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The SH3BGRL3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
SH3 domain-binding glutamic acid-rich-like protein 3 (SH3BGRL3) which is located on chromosome 1p34.3-35, encodes for a small 93 amino acids protein. SH3BGRL3 is the newest member of thioredoxin super family, whose posttranslational altered form was recognized as TNF-alpha inhibitory protein. SH3BGRL3 may act as a regulator in all-trans retinoic acid-induced pathway and also as a modulator of glutaredoxin biological activity.
Synonyms
SH3 Domain Binding Glutamic Acid-Rich Protein Like 3, SH3BGRL3-Like Protein, SH3 Domain-Binding Protein 1, SH3BP-1, TNF Inhibitory Protein, TIP-B1.
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 MGSMSGLRVY STSVTGSREI KSQQSEVTRI LDGKRIQYQL VDISQDNALR DEMRALAGNP KATPPQIVNG DQYCGDYELF VEAVEQNTLQ EFLKLA

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:

Transcription Elongation Factor A (SII)-Like 3 Human Recombinant

Transcription elongation factor A (SII)-like 3, TCEA-like protein 3, MGC15737.

Product # :

PRO-1128

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Description

TCEAL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 224 amino acids (1-200) and having a molecular mass of 25.0 kDa.TCEAL3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TCEAL3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
TCEAL3 belongs to the transcription elongation factor A (SII)-like (TCEAL) gene family. TCEAL family members hold TFA domains and operate as nuclear phosphoproteins which control transcription in a promoter context-dependent fashion. Various family members are situated in the X chromosome.
Synonyms
Transcription elongation factor A (SII)-like 3, TCEA-like protein 3, MGC15737.
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 MGSHMEKPYN KNEGNLENEG KPEDEVEPDD EGKSDEEEKP DVEGKTECEG KREDEGEPGD EGQLEDEGSQ EKQGRSEGEG KPQGEGKPAS QAKPESQPRA AEKRPAEDYV PRKAKRKTDR GTDDSPKDSQ EDLQERHLSS EEMMRECGDV SRAQEELRKK QKMGGFHWMQ RDVQDPFAPR GQRGVRGVRG GGRGQRGLHD IPYL

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:

TIMELESS Interacting Protein Human Recombinant

TIMELESS Interacting Protein, CSM3 Homolog.

Product # :

PRO-1710

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Description

TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.
Synonyms
TIMELESS Interacting Protein, CSM3 Homolog.
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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

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.

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