Search: 1000 results found for "CTGF"

Description:

Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

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CYT-679

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Description

TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
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
MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.
Background
Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.
Introduction:

TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.
Production Process and Characteristics:

TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.
Therapeutic Applications:

TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.
Advantages and Challenges:

The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.
Conclusion:

TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

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-Alpha Human Recombinant

Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.

Product # :

CYT-871

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Description

TGFA Human Recombinant (40-89) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.6kDa. The TGFA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in 0.1% TFA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured in a proliferation assay using mouse BALB/c 3T3 cells, is 0.395ng/ml.

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Introduction
Transforming Growth Factor-Alpha (TGF-alpha) belongs to the EGF family of cytokines. TGFA soluble form is discharged from the membrane by proteolytic cleavage. Membrane-bound proTGF-alpha is biologically active and has a role in cell-cell adhesion or in the stimulation of adjacent cells. TGFA expression is common in transformed cells. Additionally, TGFA is expressed in normal tissues during embryogenesis and in adult cells/tissues, including the pituitary, keratinocytes, and macrophages.
Synonyms
Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFA 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 TGFA in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA.
Background
Title: Transforming Growth Factor-Alpha Human Recombinant, Yeast: A Versatile Biopharmaceutical for Therapeutic Applications
Abstract:

Transforming Growth Factor-Alpha (TGF-α) is a potent growth factor involved in numerous physiological processes, including cell proliferation, differentiation, and tissue repair. The development of TGF-α human recombinant using yeast expression systems has provided a valuable biopharmaceutical tool for therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic applications of TGF-α human recombinant derived from yeast, highlighting its versatility and clinical significance.
Introduction:

TGF-α is a crucial growth factor that regulates cellular functions and plays a vital role in tissue development and repair. Harnessing the therapeutic potential of TGF-α has been limited by challenges in its production and stability. However, the development of TGF-α human recombinant using yeast expression systems has overcome these limitations, making it an attractive biopharmaceutical for therapeutic interventions.
Production Process and Characteristics:

TGF-α human recombinant derived from yeast is produced through recombinant DNA technology, utilizing yeast cells as expression hosts. Yeast expression systems offer several advantages, including high expression yields, cost-effectiveness, and the ability to produce correctly folded and biologically active TGF-α. The resulting TGF-α human recombinant closely resembles native TGF-α in terms of structure and function, allowing for effective therapeutic intervention.
Therapeutic Applications:

TGF-α human recombinant derived from yeast has shown promise in various therapeutic applications. It has been investigated for its wound-healing properties, where it promotes tissue regeneration and accelerates the healing process. Additionally, TGF-α has been explored in tissue engineering and regenerative medicine, playing a crucial role in stimulating cell proliferation and tissue development. Furthermore, TGF-α has been studied in the context of cancer research, as it is involved in tumor growth and angiogenesis, making it a potential target for anticancer therapies.
Advantages and Challenges:

The use of yeast expression systems for producing TGF-α human recombinant offers several advantages, including scalability, cost-effectiveness, and the ability to produce bioactive protein. However, challenges remain, such as optimizing production processes, purification methods, and ensuring product consistency and stability. Further research is needed to address these challenges and maximize the clinical potential of TGF-α human recombinant derived from yeast.
Conclusion:

TGF-α human recombinant derived from yeast represents a versatile biopharmaceutical tool with significant therapeutic potential. Its production using yeast expression systems offers advantages in terms of scalability, cost-effectiveness, and bioactivity. The therapeutic applications of TGF-α human recombinant extend to wound healing, tissue engineering, and cancer research. Continued research and development efforts are crucial to optimizing production processes, overcoming challenges, and fully exploiting the clinical benefits of TGF-α human recombinant as a therapeutic agent.

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:

Ciliary Neurotrophic Factor Rat Recombinant, His Tag

Ciliary neurotrophic factor, CNTF, Cntf.

Product # :

CYT-926

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Description

CNTF Rat Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-200a.a) and having a molecular mass of 25.2kDa.CNTF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CNTF protein solution (0.5mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.
Synonyms
Ciliary neurotrophic factor, CNTF, Cntf.
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 MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25.2kDa.

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

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

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

What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.

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

Transforming Growth Factor-Beta 3 Human Recombinant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-368

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Description

TGF-β 3 Human Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.8kDa. The TGF-β 3 is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein solution contains 20% Ethanol and 10mM Acetic acid (AcOH).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the ability to induce chondrogenic differentiation.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered clear solution.
Stability
TGF-beta 3 although stable at room temperature for 1 week, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Amino Acid Sequence
MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Background
TGFB3 (207 a.a.) Human

About TGFB3 (207 a.a.) Human:
Transforming growth factor beta-3 (also known as TGF-β3) is a cytokine encoded by the TGFB3 gene that belongs to the transforming growth factor beta superfamily. It plays a significant role in cell differentiation, embryogenesis, and development by regulating molecules involved in cell adhesion and extracellular matrix formation. TGF-β3 is necessary for palate development, as its absence causes clefting. In addition, it controls lung development and wound healing processes by regulating cell adhesion and movement in the respective tissues. Together, TGF-β3 coordinates a variety of cellular processes that are critical for mammalian embryonic development and tissue homeostasis. In this article we will explore the features and applications of TGFB3 Human Recombinant Protein, expanding on its significance in in advanced research pursuits.
Description:
TGFB3 Human Recombinant protein encodes amino acids 644-850 and total molecular mass of 50 kDa (Including GST Tag). As TGFB3 Human derives from Escherichia Coli, it appears as a sterile filtered clear solution and is formulated as 100µl of purified human TGF Beta 3 protein at 100µg/ml. In addition, its protein is formulated in a solution comprising 50mM Tris-Acetate (pH 7.5), 1mM EDTA, and 20% Glycerol. In terms of stability, TGF-beta 3 Human Recombinant is stable at 4°C for up to a week. However, it is preferable to store at -20°C. However, if you are looking to store it for a long term it is preferable to add a carrier protein (0.1% HSA or BSA).
Activation:
While TGF-β plays a crucial role regulating essential cell functions, its activation pathways is still being explored and understood. Some pathways are specific to certain cells or tissues, while others are more widespread. Factors like proteases, integrins, pH, and reactive oxygen species can activate TGF-β. Disruptions in these factors can lead to uncontrolled TGF-β signaling, causing issues like inflammation, autoimmune diseases, and cancer.
Applications and Usage:
TGFB3 (207 a.a.) Human is intended for laboratory research, serving as an important tool in stem cell differentiation as well as T-cell regulation and differentiation. Accordingly, its versatility extends to applications such as ELISA, Western Blotting, and Inhibition Assays, offering different avenues for discovery and research.
Safety Information:
TGFB3 (207 a.a.) Human is intended for use only in laboratory research, in accordance with safety guidelines. It emphasizes adherence to ethical and regulatory norms and is not intended for use as household chemicals, pharmaceuticals, agricultural products, or food additives.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TGF-b 3 as a Reference Standard.

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:

Cathepsin-F Human Recombinant

800x600 CATSF, CLN13, Cathepsin F, EC=3.4.22.41. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

Product # :

ENZ-738

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Description

800x600 CTSF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (271-484) and having a molecular mass of 26kDa.CTSF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cathepsin F ( CTSF) is a member of the peptidase C1 family. Cathepsins are papain familycysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene isubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.
Synonyms
CATSF, CLN13, Cathepsin F, EC=3.4.22.41.
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 MGSAPPEWDW RSKGAVTKVK DQGMCGSCWA FSVTGNVEGQ WFLNQGTLLS LSEQELLDCD KMDKACMGGL PSNAYSAIKN LGGLETEDDY SYQGHMQSCN FSAEKAKVYI NDSVELSQNE QKLAAWLAKR GPISVAINAF GMQFYRHGIS RPLRPLCSPW LIDHAVLLVG YGNRSDVPFW AIKNSWGTDW GEKGYYYLHR GSGACGVNTM ASSAVVD.

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:

Cathepsin-D Human Recombinant

Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

Product # :

ENZ-378

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Description

CTSD produced in HEK293 cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-412 a.a.) and having a molecular mass of 43.4kDa. CTSD is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells

Formulation

CTSD at 1mg/ml in 50mM MES, pH5.5, 100mM NaCl and 20% Glycerol.

Purity

Greater than 95% as determined by SDS-PAGE

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Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
Synonyms
Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
Amino Acid Sequence
LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RLHHHHHH
Enzymatic Activity
> 20 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-3.5 at 25C.

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:

Cathepsin-F Human Recombinant, Sf9

CTSF, CATSF, CLN13.

Product # :

ENZ-1167

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Description

CTSF produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 474 amino acids (20-484.a.a) and having a molecular mass of 52.5kDa.CTSF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CTSF protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 40% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 5 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of Z-Phe-ArgAMC to Z-Phe-Arg and AMC per minute at pH 5.0 at 37^℃.

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Introduction
Cathepsin F (CTSF) is a member of the peptidase C1 family. Cathepsins are papain family cysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF is involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.
Synonyms
CTSF, CATSF, CLN13.
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
ADLAPAQPRA ASFQAWGPPS PELLAPTRFA LEMFNRGRAA GTRAVLGLVR GRVRRAGQGS LYSLEATLEE PPCNDPMVCR LPVSKKTLLC SFQVLDELGR HVLLRKDCGP VDTKVPGAGE PKSAFTQGSA MISSLSQNHP DNRNETFSSV ISLLNEDPLS QDLPVKMASI FKNFVITYNR TYESKEEARW RLSVFVNNMV RAQKIQALDR GTAQYGVTKF SDLTEEEFRT IYLNTLLRKE PGNKMKQAKS VGDLAPPEWD WRSKGAVTKV KDQGMCGSCW AFSVTGNVEG WFLNQGTLL SLSEQELLDC DKMDKACMGG LPSNAYSAIK NLGGLETEDD YSYQGHMQSC NFSAEKAKVY INDSVELSQN EQKLAAWLAK RGPISVAINA FGMQFYRHGI SRPLRPLCSP WLIDHAVLLV GYGNRSDVPF WAIKNSWGTD WGEKGYYYLH RGSGACGVNT MASSAVVDHH HHHH

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 2 Human Recombinant, CHO

Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.

Product # :

CYT-1268

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Description

TGFB2 Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 Human 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 TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.2 ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.

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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 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 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS.
Background
Recombinant TGFB2 protein is used in cell culture to study extracellular matrix remodelling, tissue regeneration, and developmental biology.
TGFB2 takes part in embryonic development and is involved in fibrosis, wound healing, angiogenesis,

What is the molecular weight / Mw of TGFB2 Protein?
TGFB2 Protein has a total Mw of 25.4kDa.

What is the source or expression system of TGFB2 Protein?
CHO Cells

What is the Purity of TGFB2 Protein?
TGFB2 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of TGFB2 Protein?
Determined by its ability to inhibit the mouse IL4-dependent proliferation of mouse HT2 cells. The expected ED50 for this effect is less than 0.2ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.

What is the amino acid sequence of TGFB2 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS

What applications can TGFB2 Protein be used in?
TGFB2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for TGFB2 Protein?
The endotoxin level is minimal, TGFB2 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:

Transforming Growth Factor-Beta 2 Human Recombinant, HEK

Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

Product # :

CYT-112

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Description

TGF-b 2 Human Recombinant produced in HEK cells is a non-glycosylated homodimer, having a total molecular weight of 25kDa.The TGF-b 2 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

TGF-b 2 was lyophilized from a 0.2µm filtered solution containing 50mM sodium acetate pH 4.5.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2), the ED₅₀ is 0.16ng/ml.

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Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-beta (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGF-b 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 2 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 TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.

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 3 (24-412 a.a.) Human Recombinant

Transforming Growth Factor, Beta 3, Prepro-Transforming Growth Factor Beta-3, TGF-Beta-3, ARVD1, RNHF, Arrhythmogenic Right Ventricular Dysplasia 1, Transforming Growth Factor Beta-3, TGF-Beta3, ARVD, Transforming growth factor beta-3, TGF-beta-3.

Product # :

CYT-886

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Description

TGFB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (24-412 a.a) and having a molecular mass of 47.2kDa. TGFB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TGFB3 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming Growth Factor, Beta 3, Prepro-Transforming Growth Factor Beta-3, TGF-Beta-3, ARVD1, RNHF, Arrhythmogenic Right Ventricular Dysplasia 1, Transforming Growth Factor Beta-3, TGF-Beta3, ARVD, Transforming growth factor beta-3, TGF-beta-3.
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 MGSLSTCTTL DFGHIKKKRV EAIRGQILSK LRLTSPPEPT VMTHVPYQVL ALYNSTRELL EEMHGEREEG CTQENTESEY YAKEIHKFDM IQGLAEHNEL AVCPKGITSK VFRFNVSSVE KNRTNLFRAE FRVLRVPNPS SKRNEQRIEL FQILRPDEHI AKQRYIGGKN LPTRGTAEWL SFDVTDTVRE WLLRRESNLG LEISIHCPCH TFQPNGDILE NIHEVMEIKF KGVDNEDDHG RGDLGRLKKQ KDHHNPHLIL MMIPPHRLDN PGQGGQRKKR ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

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:

Cleavage Stimulation Factor 1 Human Recombinant

Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

Product # :

PRO-1170

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Description

CSTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-431 a.a) and having a molecular mass of 49.4kDa.CSTF1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CSTF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.
Synonyms
Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.
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
MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DVEHHHHHH.

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 3 (207 a.a.) Human Recombinant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-319

Price :

Quantity :

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Description

TGFB3 Human Recombinant protein encoding amino acids 644-850 and total molecular mass of 50 kDa (Including GST Tag).

Source

Escherichia Coli.

Formulation

100µl purified human TGF Beta 3protein at 100µg/ml in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol.

More Info

Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered clear solution.
Stability
TGF-beta 3 Human Recombinant although stable at 4°C for 1 week, should be stored at -20°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze-thaw cycles.
Applications
(a) ELISA.
(b) Western Blotting.
(c) Inhibition Assays.

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:

Cholera Toxin B subunit Recombinant

Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.

Product # :

PRO-2605

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Description

Cholera Toxin B subunit Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 103 amino acids and having a molecular mass of 11.6kDa.ctxB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ctxB is supplied as a 0.2 μm filtered solution conteining 5mM PB, pH 7.0, 75mM NaCl, and 50 % glycerol.

Purity

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

More Info

Introduction
Cholera Toxin B subunit (ctxB) Cholera is a protein complex secreted by the bacterium Vibrio cholerae. ctxB is responsible for the massive, watery diarrhea characteristic of cholera infection. The cholera toxin is an oligomeric complex made up of 6 protein subunits: a single copy of the A subunit and5 copies of the B subunit, denoted as AB5. Subunit B binds while subunit A activates the G protein which activates adenylate cyclase. The five B subunits form a five-membered ring. The A subunit has 2 important segments. The A1 portion of the chain (CTA1) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2) forms an extended alpha helix which sits snugly in the central pore of the B subunit ring.
Synonyms
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
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
TPQNITDLCA EYHNTQIYTL NDKIFSYTES LAGKREMAII TFKNGAIFQV EVPGSQHIDS QKKAIERMKD TLRIAYLTEA KVEKLCVWNN KTPHAIAAIS MAN.

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:

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Product # :

CYT-1095

Price :

Quantity :

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Shipped at Room temp

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Description

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 128 amino acids and having a molecular mass of 14.5kDa. GMCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.

More Info

Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of GMCSF is found extracellularly as a homodimer. GMCSF has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.
Background
What is the molecular weight/Mw of GM-CSF PORCINE Protein?
GM-CSF PORCINE Protein has a total Mw of 14.5kDa.

What is the source or expression system of GM-CSF PORCINE Protein?
Escherichia Coli.

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

What is the Biological Activity of GM-CSF PORCINE Protein?
The ED50, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.

What is the amino acid sequence of GM-CSF PORCINE Protein?
MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.

What applications can GM-CSF PORCINE Protein be used in?
GM-CSF PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF PORCINE Protein?
The endotoxin level is minimal, GM-CSF PORCINE 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:

Transforming Growth Factor-Beta 3 Mouse Recombinant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-143

Price :

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Description

TGF-β 3 Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.7kDa. The TGF-β 3 is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse TGFB3 protein solution contains 20% Ethanol and 10mM Acetic acid.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the ability to induce chondrogenic differentiation.

More Info

Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered clear solution.
Stability
Mouse TGF-beta 3 although stable at room temperature for 3 weeks, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Amino Acid Sequence
MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TGF-b 3 as a Reference Standard.

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 3 Human Recombinant, CHO

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-1259

Price :

Quantity :

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Shipped at Room temp

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Description

TGFB3 Human Recombinant produced in CHO cells is a glycosylated, polypeptide homodimer chain containing 2x112 amino acids and having a total molecular mass of 25.0kDa. The TGFB3 is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

TGFB3 was lyophilized from a concentrated solution containing 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0 × 10⁷ units/mg.

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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Transforming Growth Factor-Beta 3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 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 TGFB3 in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Background
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

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:

Insulin Like Growth Factor-1 N15 Labeled Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-128

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Description

IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled. The IGF1 N15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 N15 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

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 serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

sds-page

More Info

Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 N15 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 IGF1 N15 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
Background
What is the molecular weight/Mw of IGF1 N15 HUMAN Protein?
IGF1 N15 HUMAN Protein has a total Mw of 7.74kDa.

What is the source or expression system of IGF1 N15 HUMAN Protein?
Escherichia Coli.

What is the Purity of IGF1 N15 HUMAN Protein?
IGF1 N15 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 N15 HUMAN Protein?
The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

What is the amino acid sequence of IGF1 N15 HUMAN Protein?
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

What applications can IGF1 N15 HUMAN Protein be used in?
IGF1 N15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 N15 HUMAN Protein?
The endotoxin level is minimal, IGF1 N15 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:

Granulocyte Macrophage-Colony Stimulating Factor Rat Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Product # :

CYT-395

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Granulocyte Macrophage Colony Stimulating Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14590.65 Dalton. GM-CSF Rat Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GM-CSF Rat was lyophilized with no additives.

Purity

Greater than 96.0% as determined by:
(a)Analysis by RP-HPLC.
(b)Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×10⁸units/mg.

More Info

Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
VTTFEDFIKN LKGFLFDIPF DCWKPVQK.
Background
What is the molecular weight/Mw of GM-CSF RAT Protein?
GM-CSF RAT Protein has a total Mw of 14.59kDa.

What is the source or expression system of GM-CSF RAT Protein?
Escherichia Coli.

What is the Purity of GM-CSF RAT Protein?
GM-CSF RAT Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF RAT Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.

What is the amino acid sequence of GM-CSF RAT Protein?
MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
VTTFEDFIKN LKGFLFDIPF DCWKPVQK.

What applications can GM-CSF RAT Protein be used in?
GM-CSF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF RAT Protein?
The endotoxin level is minimal, GM-CSF RAT 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:

Trefoil Factor-3 Rat Recombinant

Trefoil factor 3, Intestinal trefoil factor, rITF, Polypeptide P1.B, rP1.B, Tff3, Itf.

Product # :

CYT-781

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Description

The Trefoil Factor-3 Rat was constructed as a recombinant protein with a 9 a.a C-terminal fusion of Flag-Tag (1 aa N-terminal+8 aa C-terminal). The TFF3 Rat produced in E.coli, is 7.7kDa protein containing a total of 68 amino acid residues.

Source

Escherichia Coli.

Formulation

TFF3 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM TRIS and 50mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.
Synonyms
Trefoil factor 3, Intestinal trefoil factor, rITF, Polypeptide P1.B, rP1.B, Tff3, Itf.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein 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 0.5 mg/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
MQEFVGLSPS QCMVPANVRV DCGYPTVTSE QCNNRGCCFD SSIPNVPWCF KPLQETECT F DYKDDDDK.

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:

Trefoil Factor-1 Human Recombinant

TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

Product # :

CYT-586

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Description

TFF-1 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 60 amino acids which includes a 40 amino acid trefoil motif containing 3 conserved intramolecular disulfide bonds and having a total molecular mass of 13.2 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Human TFF1 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 150mM NaCl.

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 chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

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Introduction
The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.
Synonyms
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TFF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 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 TFF1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFY
PNTIDVPPEEECEF.

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:

Osteoprotegerin Human Recombinant /Fc Chimera

TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

Product # :

CYT-266

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Description

Recombinant OPG produced in yeast contains 2x412 amino acid residues, including 180 residues from mature OPG (a.a 22-201) and 232 residues from the Fc protein of human IgG1, and has a calculated molecular mass of 109.6kDa.

Source

Pichia Pastoris.

Formulation

OPG was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 6.0, 150mM NaCl and 0.02 % Tween-80.

Purity

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

Biological Activity

The ED₅₀ as determined by neutralizing the stimulation of U937 cells is less tha10ng/ml, corresponding to a specific activity of > 1.0 × 10⁵IU/mg in the presence of 10ng/ml soluble Human RANKL (sRANKL).

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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
OPG 22-201 ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQKCGIDVTL
Fc232EPKSSDKTHT CPPCPAPEFE GAPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPTPIEKTISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK

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:

Canopy 3 Homolog Human Recombinant

CAG4A, ERDA5, PRAT4A, TNRC5, Protein canopy homolog 3, CTG repeat protein 4a, Expanded repeat-domain protein CAG/CTG 5, Protein associated with TLR4, Trinucleotide repeat-containing gene 5 protein,CNPY3.

Product # :

PRO-1386

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CNPY3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (31-278 a.a.) and having a molecular mass of 29.9kDa. CNPY3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CNPY3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
Canopy 3 homolog (CNPY3) is a 271 a.aToll-like receptor specific co-chaperone for HSP90B1. CNPY3 is necessitated for proper TLR folding, excluding that of TLR3, and so controls TLR exit from the endoplasmic reticulum. Therefore, CNPY3i s required for both innate and adaptive immune responses.
Synonyms
CAG4A, ERDA5, PRAT4A, TNRC5, Protein canopy homolog 3, CTG repeat protein 4a, Expanded repeat-domain protein CAG/CTG 5, Protein associated with TLR4, Trinucleotide repeat-containing gene 5 protein,CNPY3.
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 MGSGPSQAGA EENDWVRLPS KCEVCKYVAV ELKSAFEETG KTKEVIGTGY GILDQKASGV KYTKSDLRLI EVTETICKRL LDYSLHKERT GSNRFAKGMS ETFETLHNLV HKGVKVVMDI PYELWNETSA EVADLKKQCD VLVEEFEEVI EDWYRNHQEE DLTEFLCANH VLKGKDTSCL AEQWSGKKGD TAALGGKKSK KKSSRAKAAG GRSSSSKQRK ELGGLEGDPS PEEDEGIQKA SPLTHSPPDE L.

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 Receptor Associated Protein 1 Human Recombinant

TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.

Product # :

PRO-1890

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Description

TGFBRAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (601-860 a.a) and having a molecular mass of 33kDa.TGFBRAP1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TGFBRAP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

More Info

Introduction
TGF-beta receptor-associated protein 1 also known as TGFBRAP1 takes part in the TGF-beta/activin signaling pathway. TGFBRAP1 is related with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. TGFBRAP1recruits SMAD4 to the vicinity of the receptor complex and smoothes the progress of its interaction with receptor-regulated Smads, such as SMAD2.
Synonyms
TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSKRLQ KEEYHTHLAV LYLEEVLLQR ASASGKGAEA TETQAKLRRL LQKSDLYRVH FLLERLQGAG LPMESAILHG KLGEHEKALH ILVHELQDFA AAEDYCLWCS EGRDPPHRQQ LFHTLLAIYL HAGPTAHELA VAAVDLLNRH ATEFDAAQVL QMLPDTWSVQ LLCPFLMGAM RDSIHARRTM QVALGLARSE NLIYTYDKMK LKGSSIQLSD KKLCQICQNP FCEPVFVRYP NGGLVHTHCA ASRHTNPSSS SPGTRT

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 Human Recombinant, His Tag

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.

Product # :

CYT-672

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TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (279-390) having a molecular weight of 17.3kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TGF-b 1 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TGF-b 1 His-Tag protein is supplied in 25mM NaAcetate pH 4.8 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
TGF-b 1 regulates the actions of numerous other growth factors involved in a variety of human diseases including renal disease, hepatic disease, heart failure and cardiomyopathies.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.
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. Please avoid 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.

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