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1000 results found for “VEGF Protein”
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Name :
PLGF 2 Human, Sf9Description:
Recombinant Human Placental Growth Factor-2, Sf9
PIGF, PGF, PlGF-2, PLGF-2.
Product # :
CYT-420Price :
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Shipped at Room temp
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Description
Placenta Growth Factor-2 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 152 amino acids and having a total molecular mass of 44 kDa. The PLGF-2 is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing BSA.
Purity
Greater than 80.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
PlGF-2 human Recombinant can bind to immobilized rh-sFlt-1 (100ng/well) with a linear range at 0.3–10ng/ml.More Info
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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
PLGF-2 binds neuropilin-1 and 2 in a dependent manner. -
Synonyms
PIGF, PGF, PlGF-2, PLGF-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Placenta Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF2 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Placenta Growth Factor 2 in sterile 20mM acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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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Name :
MANF Human, HisDescription:
Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant, His Tag
Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.
Product # :
CYT-133Price :
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Description
MANF Human Recombinant produced in E. coli is a single polypeptide chain containing 183 amino acids (25-182) and having a molecular mass of 20.8kDa.MANF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MANF solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.
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Synonyms
Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLRPGD CEVCISYLGR FYQDLKDRDV TFSPATIENE LIKFCREARG KENRLCYYIG ATDDAATKII NEVSKPLAHH IPVEKICEKL KKKDSQICEL KYDKQIDLST VDLKKLRVKE LKKILDDWGE TCKGCAEKSD YIRKINELMP KYAPKAASAR TDL
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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Name :
ZNF689 HumanDescription:
Zinc Finger Protein 689 Human Recombinant
Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.
Product # :
PRO-1737Price :
Quantity :
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Description
ZNF689 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (1-500a.a) and having a molecular mass of 59.3kDa.ZNF689 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZNF689 protein solution (1.0mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Zinc Finger Protein 689 (ZNF689) is a member of the krueppel C2H2-type zinc-finger protein family. The ZNF689 protein contains 12 C2H2-type zinc fingers and 1 KRAB domain. ZNF689 may be involved in transcriptional regulation.
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Synonyms
Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPPSAP LPAQGPGKAR PSRKRGRRPR ALKFVDVAVY FSPEEWGCLR PAQRALYRDV MRETYGHLGA LGCAGPKPAL ISWLERNTDD WEPAALDPQE YPRGLTVQRK SRTRKKNGEK EVFPPKEAPR KGKRGRRPSK PRLIPRQTSG GPICPDCGCT FPDHQALESH KCAQNLKKPY PCPDCGRRFS YPSLLVSHRR AHSGECPYVC DQCGKRFSQR KNLSQHQVIH TGEKPYHCPD CGRCFRRSRS LANHRTTHTG EKPHQCPSCG RRFAYPSLLA IHQRTHTGEK PYTCLECNRR FRQRTALVIH QRIHTGEKPY PCPDCERRFS SSSRLVSHRR VHSGERPYAC EHCEARFSQR STLLQHQLLH TGEKPYPCPD CGRAFRRSGS LAIHRSTHTE EKLHACDDCG RRFAYPSLLA SHRRVHSGER PYACDLCSKR FAQWSHLAQH QLLHTGEKPF PCLECGRCFR QRWSLAVHKC SPKAPNCSPR SAIGGSSQRG NAH.
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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Name :
ANGPT1 HumanDescription:
Angiopoietin-1 Human Recombinant
Angiopoietin 1, KIAA0003, ANG-1, AGP1, AGPT.
Product # :
CYT-074Price :
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Shipped with Ice Packs
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Description
ANGPT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (20-498) and having a molecular mass of 55.6 kDa.The ANGPT1 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ANGPT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 5% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
ANGPT1 is an angiogenic factor which intervenes in blood vessel maturation and takes part in endothelial development. ANGPT1 is a secreted ligand for Tie-2, a cell surface receptor tyrosine kinase expressed in endothelial and hemopoietic cells. The glycosylated ANGPT1 protein has a coiled-coil region in the amino terminus and a fibrinogen-like domain at the carboxy terminus.
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Synonyms
Angiopoietin 1, KIAA0003, ANG-1, AGP1, AGPT.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MSNQRRSPEN SGRRYNRIQH GQCAYTFILP EHDGNCREST TDQYNTNALQ RDAPHVEPDF SSQKLQHLEH VMENYTQWLQ KLENYIVENM KSEMAQIQQN AVQNHTATML EIGTSLLSQT AEQTRKLTDV ETQVLNQTSR LEIQLLENSL STYKLEKQLL QQTNEILKIH EKNSLLEHKI LEMEGKHKEE LDTLKEEKEN LQGLVTRQTY IIQELEKQLN RATTNNSVLQ KQQLELMDTV HNLVNLCTKE GVLLKGGKRE EEKPFRDCAD VYQAGFNKSG IYTIYINNMP EPKKVFCNMD VNGGGWTVIQ HREDGSLDFQ RGWKEYKMGF GNPSGEYWLG NEFIFAITSQ RQYMLRIELM DWEGNRAYSQ YDRFHIGNEK QNYRLYLKGH TGTAGKQSSL ILHGADFSTK DADNDNCMCK CALMLTGGWW FDACGPSNLN GMFYTAGQNH GKLNGIKWHY FKGPSYSLRS TTMMIRPLDF
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Background
This factor was found in the conditioned medium of the human neuroepithelioma cell line SHEP1 and the mouse myoblast cell line C2C12ras. The cDNA encoding a protein of 498 amino acids was isolated by using a secretion-trap expression cloning procedure exploiting the presence of a signal sequence present in growth factors that are secreted by producer cells (Davis et al, 1996). Murine and human factors show 97 % identity at the amino acid level. For a related factor see: CDT6. The human gene has been mapped to chromosome 8q22.3-q23 (Cheung et al, 1998).
The expression of angiopoietin-1 mRNA is downregulated by PDGF, EGF, IL1-beta, and TGF-beta (Enholm et al, 1997).
Angiopoietin-1 is a ligand for the receptor-like tyrosine kinase designated TIE-2 (Davis et al, 1996). Binding of Angiopoietin-1 to its receptor induces tyrosine phosphorylation of the cytoplasmic receptor domain. A naturally occuring antagonist of Angiopoietin-1 binding to TIE-2 is Angiopoietin-2. Angiopoietin-1 also binds to the TIE-1 receptor and this interaction appears to be critical for the development of the right-hand side venous system. It is dispensable for the left-hand side venous system, suggesting that right-hand and left-hand side vascular networks are established early before asymmetrical features of the network become morphologically discernible Loughna and Sato, 2001).
Angiopoietin-1 does not directly promote the growth of cultured endothelial cells. Angiopoietin-1 is chemotactic for endothelial cells (Witzenbichler et al, 1998). Excess soluble TIE-2 receptors abolish the chemotactic response of endothelial cells toward angiopoietin-1. Angiopoietin-1 has been shown to counteract cell death by apoptosis in cultured endothelial cells (Holash et al, 1999). Angiopoietin-1 also acts as an apoptosis survival factor for endothelial cells and this effect is augmented by the presence of VEGF (Kwak et al, 1999).
Angiopoietin-2 dose-dependently blocks directed migration toward Angiopoietin-1. Carlson et al (2001) have shown that Ang-1 binds rather selectively to vitronectin and that Ang-1 can directly support adhesion of human umbilical vein endothelial cells and fibroblasts in a process mediated by integrins.
The physiologic roles of Angiopoietin-1 and its receptor are limited to angiogenic processes that occur subsequent to the earlier vasculogenic and angiogenic actions of the VEGF family and their receptors. However, it is unlike most of the known angiogenesis factors such as VEGF and other classical endothelial cell growth factors in that addition of the factor to cultures of endothelial cells does not directly promote cell growth even though the TIE-2 receptor becomes activated. Angiopoietin-1 also appears to be incapable of inducing the formation of tubules by endothelial cells.
Angiopoietins can potentiate the effects of other angiogenic cytokines. An investigation of the impact of angiopoietins on neovascularization in vivo in the cornea micropocket assay of neovascularization demonstrates that neither Angiopoietin-1 nor Angiopoietin-2 alone promote neovascularization. Holash et al (1999) have shown that a subset of tumors initially grows by coopting existing host vessels. Regression of these vessels via a process that involves disruption of interactions between endothelial cells and smooth muscle cells as well as cell death by apoptosis of endothelial cells first causes loss of tumour cells before angiogenesis begins at the tumor margin and the tumor is rescued under the influence of VEGF, Angiopoietin-1, and probably other angiogenic stimuli.
The embryonic expression pattern of Angiopoietin-1 suggests that it plays a particularly important role in the developing heart. Angiopoietin-1 is expressed highly in the myocardial wall surrounding the endocardium expressing TIE-2. Expression of Angiopoietin-1 becomes much more widespread later in development.
ANGPT1 Protein has a total Mw of 55.6kDa.
What is the source or expression system of ANGPT1 Protein?
Escherichia Coli.
What is the Purity of ANGPT1 Protein?
ANGPT1 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPT1 Protein?
The biological functionality of ANGPT1 Protein will be determined in the future.
What is the amino acid sequence of ANGPT1 Protein?
MSNQRRSPEN SGRRYNRIQH GQCAYTFILP EHDGNCREST TDQYNTNALQ RDAPHVEPDF SSQKLQHLEH VMENYTQWLQ KLENYIVENM KSEMAQIQQN AVQNHTATML EIGTSLLSQT AEQTRKLTDV ETQVLNQTSR LEIQLLENSL STYKLEKQLL QQTNEILKIH EKNSLLEHKI LEMEGKHKEE LDTLKEEKEN LQGLVTRQTY IIQELEKQLN RATTNNSVLQ KQQLELMDTV HNLVNLCTKE GVLLKGGKRE EEKPFRDCAD VYQAGFNKSG IYTIYINNMP EPKKVFCNMD VNGGGWTVIQ HREDGSLDFQ RGWKEYKMGF GNPSGEYWLG NEFIFAITSQ RQYMLRIELM DWEGNRAYSQ YDRFHIGNEK QNYRLYLKGH TGTAGKQSSL ILHGADFSTK DADNDNCMCK CALMLTGGWW FDACGPSNLN GMFYTAGQNH GKLNGIKWHY FKGPSYSLRS TTMMIRPLDF
What applications can ANGPT1 Protein be used in?
ANGPT1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPT1 Protein?
The endotoxin level is minimal, ANGPT1 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.
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Name :
Protein-L Cys, HisDescription:
Protein-L Cys Recombinant, His Tag
Product # :
PRO-1932Price :
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Shipped at Room temp
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Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus and a Cys on C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 373 amino acids in total and having a molecular mass of 41.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 96.0% as determined by SDS-PAGE.
More Info
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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.
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Solubility
It is recommended to reconstitute the lyophilized Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AGC.
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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Name :
TGFB1 (113 a.a.) HumanDescription:
Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
Product # :
CYT-679Price :
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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.
More Info
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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.
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Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.
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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.
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Name :
SCGB1D1 HumanDescription:
Secretoglobin Family 1D, Member 1 Human Recombinant
Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA.
Product # :
PRO-1602Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SCGB1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-90) containing 79 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 8.8kDa (calculated).
Source
Escherichia Coli.
Formulation
SCGB1D1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Secretoglobin Family 1D, Member 1 (SCGB1D1) belongs to the lipophilin subfamily, part of the uteroglobin superfamily, and is an ortholog of prostatein (which is the major secretory glycoprotein of the rat ventral prostate gland). SCGB1D1 binds androgens and other steroids. In addition SCGB1D1 binds chemotherapeutic drugs during the prostate cancer treatment. Steroid hormones regulate the SCGB1D1 transcription. SCGB1D1 is secreted into extracellular space. SCGB1D1 gene product represents one component of a heterodimeric molecule found in human tears whose elution profile is consistent with prostatein (which is a tetrameric molecule comprised of 3 peptide components in heterodimers).
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Synonyms
Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1D1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS VVCQALGSEI TGFLLAGKPV FKFQLAKFKA PLEAVAAKME VKKCVDTMAY EKRVLITKTL GKIAEKCDR.
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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Name :
PDCD1 Human, ActiveDescription:
Programmed Cell Death 1 Human Recombinant, Active
Programmed cell death protein 1, CD279, hPD-1, SLEB2, hPD-l, hSLE1, PD-1, PD1, PDCD1.
Product # :
PRO-2724Price :
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Description
PDCD1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 383 amino acids (21-170 a.a) and having a molecular mass of 42.9kDa.PDCD1 is fused to a 233 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PDCD1 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human PD-L1/B7-H1
More Info
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Introduction
PDCD1 is a cell surface membrane protein of the immunoglobulin superfamily. PDCD1 is expressed in pro-B-cells and is thought to have a role in their differentiation. In mice, expression of PDCD1 gene is induced in the thymus when anti-CD3 antibodies are injected and large numbers of thymocytes undergo apoptosis. Mice deficient for the PDCD1 gene bred on a BALB/c background developed dilated cardiomyopathy and died from congestive heart failure. These studies suggest that the PDCD1 gene product may also be important in T cell function and contribute to the prevention of autoimmune diseases.
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Synonyms
Programmed cell death protein 1, CD279, hPD-1, SLEB2, hPD-l, hSLE1, PD-1, PD1, PDCD1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
PGWFLDSPDR PWNPPTFSPA LLVVTEGDNA TFTCSFSNTS ESFVLNWYRM SPSNQTDKLA AFPEDRSQPG QDCRFRVTQL PNGRDFHMSV VRARRNDSGT YLCGAISLAP KAQIKESLRA ELRVTERRAE VPTAHPSPSP RPAGQFQTLV LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK
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.
- View Data Sheet
Name :
EIF3K HumanDescription:
Eukaryotic Translation Initiation Factor 3K Human Recombinant
Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.
Product # :
PRO-179Price :
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Description
EIF3K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218a.a.) and having a molecular mass of 27.2 kDa. EIF3K is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF3K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
EIF3K is a member of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a number of other subunits of eIF3 and the 40S ribosomal subunit. EIF3K is conserved among high eukaryotes, including mammals, insects, and plants, and it is universally expressed in human tissues. EIF3K is distributed both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4 (Cdk4).
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Synonyms
Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN IVEKIDFDSV SSIMASSQ
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.
- View Data Sheet
Name :
HAND1 HumanDescription:
Heart and Neural Crest Derivatives Expressed 1 Human Recombinant
Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.
Product # :
PRO-1231Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HAND1 Human Recombinant produced in E. coli is a single polypeptide chain containing 238 amino acids (1-215) and having a molecular mass of 26.0 kDa.HAND1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HAND1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
HAND1 is a member of the basic helix-loop-helix family of transcription factors. HAND1 is one of two HAND proteins, two closely related family members that are irregularly expressed in the emerging ventricular chambers and have a key part in cardiac morphogenesis. Operating in a complementary manner, they work in the development of the right ventricle and aortic arch arteries, implicating them as mediators of congenital heart disease. Furthermore, HAND1 is obligatory for early trophoblast differentiation.
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Synonyms
Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNLVGSY AHHHHHHHPH PAHPMLHEPF LFGPASRCHQ ERPYFQSWLL SPADAAPDFP AGGPPPAAAA AATAYGPDAR PGQSPGRLEA LGGRLGRRKG SGPKKERRRT ESINSAFAEL RECIPNVPAD TKLSKIKTLR LATSYIAYLM DVLAKDAQSG DPEAFKAELK KADGGRESKR KRELQQHEGF PPALGPVEKR IKGRTGWPQQ VWALELNQ
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.
- View Data Sheet
Name :
Leptin-A TilapiaDescription:
Leptin-A Tilapia Recombinant
Product # :
CYT-1109Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
- purity
- biological activity
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Description
Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
More Info
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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-A Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-A Tilapia 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.
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Solubility
It is recommended to reconstitute the lyophilized Leptin-A Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
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.
- View Data Sheet
Name :
CCDC25 HumanDescription:
Coiled-Coil Domain Containing 25 Human Recombinant
Coiled-coil domain-containing protein 25, CCDC25.
Product # :
PRO-1655Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CCDC25 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.9kDa.CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CCDC25 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.
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Synonyms
Coiled-coil domain-containing protein 25, CCDC25.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVFYFTS SSVNSSAYTI YMGKDKYENE DLIKHGWPED IWFHVDKLSS AHVYLRLHKG ENIEDIPKEV LMDCAHLVKA NSIQGCKMNN VNVVYTPWSN LKKTADMDVG QIGFHRQKDV KIVTVEKKVN EILNRLEKTK VERFPDLAAE KECRDREERN EKKAQIQEMK KREKEEMKKK REMDELRSYS SLMKVENMSS NQDGNDSDEF M.
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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Name :
Resistin Human (64-110)Description:
Resistin (64-110) Human Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.
Product # :
CYT-1232Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Resistin 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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.
Resistin Function
Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.
Regulation
Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.
Clinical Relevance
Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.
Resistin Mechanism
Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.
Research
Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.
Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.
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.
- View Data Sheet
Name :
SEPX1 HumanDescription:
Selenoprotein X 1 Human Recombinant
Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.
Product # :
PRO-260Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SEPX1 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 136 amino acids (1-116 a.a.) and having a molecular mass of 14.8kDa. In bacteria, the selenocystein (Sec/U) element is positioned directly following the UGA codon within the reading frame for the selenoprotein so we mutated Sec-95 to Cys. The SEPX1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SEPX1 solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT, 0.1mM PMSF, 2mM EDTA and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Methionine sulfoxide reductase B1 (SEPX1 or MSRB1), is a selenoprotein that contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that usually signals translation termination. SEPX1 is a member of the methionine sulfoxide reductase B (MsrB) family, and is expressed in an assortment of adult and fetal tissues. MSRs (Methionine sulfoxide reductases) catalyze the reduction of free and protein-bound methionine sulfoxides to corresponding methionines. The oxidation of methionine by ROS creates a diastereomeric mixture of methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO). Two separate enzyme families evolved for reduction of these sulfoxides, with methionine-S-sulfoxide reductase (MsrA) being stereospecific for Met-S-SO and methionine-R-sulfoxide reductase (MsrB) for Met-R-SO.
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Synonyms
Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE HNRSEALKVS CGKCGNGLGH EFLNDGPKPG QSRFCIFSSS LKFVPKGKET SASQGH.
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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Name :
EnfuvirtideDescription:
Enfuvirtide (T-20)
Product # :
PRO-376Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Enfuvirtide has an amino acid sequence Ac-Tyr-Thr-Ser-Leu-Ile-His-Ser-Leu-Ile-Glu-Glu-Ser-Gln-Asn-Gln-Gln-Glu-Lys-Asn-Glu-Gln-Glu-Leu-Leu-Glu-Leu-Asp-Lys-Trp-Ala-Ser-Leu-Trp-Asn-Trp-Phe-NH2, molecular formula of C204H301N51O64 and a molecular weight of 4488.9 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
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Introduction
Enfuvirtide also called human immunodeficiency fusion inhibitor blocks HIV’s ability to infect healthy CD4 cells. It can reduce the amount of HIV in the blood and increase the number of CD4 cells. Enfuvirtide operates by disrupting the HIV-1 molecular machinery at the final phase of fusion with the target cell, preventing uninfected cells from becoming infected. Enfuvirtide mimics components of the HIV-1 fusion apparatus and displace them, preventing normal fusion. HIV attaches to the host CD4+ cell receptor using the viral protein GP120; upon binding, GP120 deforms allowing the viral protein GP41 to insert itself into the host cell's plasma membrane. Entry inhibitors bind to GP41 preventing the formation of an entry pore for the capsid of the virus, keeping it out of the cell.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Enfuvirtide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Enfuvirtide 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.
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Solubility
Enfuvirtide lyophilized powder is soluble in water at a concentration of 1mg/ml.
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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Name :
PVALB HumanDescription:
Parvalbumin Human Recombinant
Parvalbumin alpha, PVALB, D22S749, MGC116759.
Product # :
PRO-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PVALB Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-110 a.a.) and having a molecular mass of 14.6kDa. The PVALB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PVALB solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Parvalbumin alpha (PVALB) is a member of a larger group of EF hand proteins. PVALB is a high affinity calcium ion-binding protein which is structurally and functionally similar to calmodulin and troponin C. Parvalbumin is expressed in a specific population of GABAergic interneurones which are believed to have a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus.
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Synonyms
Parvalbumin alpha, PVALB, D22S749, MGC116759.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSMTDL LNAEDIKKAV GAFSATDSFD HKKFFQMVGLKKKSADDVKK VFHMLDKDKS GFIEEDELGF ILKGFSPDAR DLSAKETKML MAAGDKDGDG KIGVDEFSTL VAES.
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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Name :
SVIP HumanDescription:
Small VCP/P97-Interacting Protein Human Recombinant
Small VCP/P97-Interacting Protein, SVIP.
Product # :
PRO-472Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SVIP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77) and having a molecular mass of 10.8 kDa.SVIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SVIP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 2mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Small VCP/p97-interacting protein (SVIP) is involved in various cellular processes, including membrane fusion and ubiquitin-dependent protein degradation. SVIP functions as an inhibitor of the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. On the other hand, SVIP overexpression increased the levels of p62 protein and enhanced starvation-activated autophagy as well as stimulated sequestration of polyubiquitinated proteins and p62 in autophagosomes.
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Synonyms
Small VCP/P97-Interacting Protein, SVIP.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGLCFPC PGESAPPTPD LEEKRAKLAE AAERRQKEAA SRGILDVQSV QEKRKKKEKI EKQIATSGPP PEGGLRWTVS.
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.
- View Data Sheet
Name :
ARMC10 HumanDescription:
Armadillo Repeat Containing 10 Human Recombinant
Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.
Product # :
PRO-1453Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.
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Synonyms
Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.
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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Name :
SCG3 HumanDescription:
Secretogranin III Human Recombinant
Secretogranin III, secretogranin-3, SGIII.
Product # :
PRO-1556Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SCG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 472 amino acids (20-468) and having a molecular mass of 53.0kDa.SCG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SCG3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SCG3 belongs to the chromogranin/secretogranin family of neuroendocrine secretory proteins. Though, the function of SCG3 is unknown, Granins operate as precursors for biologically active peptides. Several granins are known to serve as helper proteins in sorting and proteolytic processing of prohormones.
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Synonyms
Secretogranin III, secretogranin-3, SGIII.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFPKPGGS QDKSLHNREL SAERPLNEQI AEAEEDKIKK TYPPENKPGQ SNYSFVDNLN LLKAITEKEK IEKERQSIRS SPLDNKLNVE DVDSTKNRKL IDDYDSTKSG LDHKFQDDPD GLHQLDGTPL TAEDIVHKIA ARIYEENDRA VFDKIVSKLL NLGLITESQA HTLEDEVAEV LQKLISKEAN NYEEDPNKPT SWTENQAGKI PEKVTPMAAI QDGLAKGEND ETVSNTLTLT NGLERRTKTY SEDNFEELQY FPNFYALLKS IDSEKEAKEK ETLITIMKTL IDFVKMMVKY GTISPEEGVS YLENLDEMIA LQTKNKLEKN ATDNISKLFP APSEKSHEET DSTKEEAAKM EKEYGSLKDS TKDDNSNPGG KTDEPKGKTE AYLEAIRKNI EWLKKHDKKG NKEDYDLSKM RDFINKQADA YVEKGILDKE EAEAIKRIYS SL.
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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Name :
ESM1 Human, SF9Description:
Endothelial Cell-Specific Molecule 1 Human Recombinant, Sf9
Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.
Product # :
PRO-2588Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ESM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 174 amino acids (20-184a.a.) and having a molecular mass of 19.2kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). ESM1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ESM1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ESM1, also knows as, Endothelial cell-specific molecule 1 is a protein encoded by a gene called ESM1 in humans. ESM1 is a secreted protein that is highly expressed in human kidney and lung tissues (in the endothelial cells). There are suggestions regarding the protein’s involvement in endothelium-dependent pathological diseases, due to his regulation that is performed by cytokines.
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Synonyms
Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
ADLWSNNYAV DCPQHCDSSE CKSSPRCKRT VLDDCGCCRV CAAGRGETCY RTVSGMDGMK CGPGLRCQPS NGEDPFGEEF GICKDCPYGT FGMDCRETCN CQSGICDRGT GKCLKFPFFQ YSVTKSSNRF VSLTEHDMAS GDGNIVREEV VKENAAGSPV MRKWLNPRHH 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.
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Name :
FGF19 Human, HEKDescription:
Fibroblast Growth Factor-19 Human Recombinant, HEK
fibroblast growth factor 19, FGF19.
Product # :
CYT-1180Price :
Quantity :
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Description
FGF19 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 23-216) containing 205 amino acids and having a molecular mass of 23.0 kDa.FGF19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
FGF19 protein (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 20% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Fibroblast Growth Factor-19 (FGF-19) is a member of the FGF family. FGF-19 interacts with FGFR1, FGFR2, FGFR3 and FGFR4. T FGF-19 takes part in the suppression of bile acid biosynthesis through downregulation of CYP7A1 expression, following positive regulation of the JNK and EPK1/2 cascades. FGF-19 stimulates glucose uptake in adiposytes and is a high affinity, heparin dependent ligand for FGFR4.
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Synonyms
fibroblast growth factor 19, FGF19.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH
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Background
What is the molecular weight/Mw of FGF19 HUMAN,HEK Protein?
FGF19 HUMAN,HEK Protein has a total Mw of 23kDa.
What is the source or expression system of FGF19 HUMAN,HEK Protein?
HEK293 cells.
What is the Purity of FGF19 HUMAN,HEK Protein?
FGF19 HUMAN,HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF19 HUMAN,HEK Protein?
The biological functionality of FGF19 HUMAN,HEK Protein will be determined in the future.
What is the amino acid sequence of FGF19 HUMAN,HEK Protein?
DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH
What applications can FGF19 HUMAN,HEK Protein be used in?
FGF19 HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF19 HUMAN,HEK Protein?
The endotoxin level is minimal, FGF19 HUMAN,HEK 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.
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Name :
EFNA5 HumanDescription:
Ephrin A5 Human Recombinant
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
Product # :
PRO-2327Price :
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Description
EFNA5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 422 amino acids (21-203 a.a.) and having a molecular mass of 48.1kDa. EFNA5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNA5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.
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Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
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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Name :
S100A8 HumanDescription:
S100 Calcium Binding Protein A8 Human Recombinant
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-800Price :
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Description
S100A8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (1-93 a.a.) and having a molecular mass of 10.8 kDa. The S100A8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The S100A8 solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
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Physical Appearance
Sterile Filtered clear colorless solution.
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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.
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Amino Acid Sequence
MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.
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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Name :
ATG4B HumanDescription:
ATG4 Autophagy Related 4 Homolog B Human Recombinant
Cysteine protease ATG4B, AUT-like 1 cysteine endopeptidasem, Autophagin-1, Autophagy-related cysteine endopeptidase 1, Autophagy-related protein 4 homolog B, hAPG4B, ATG4B, APG4B, AUTL1, KIAA0943.
Product # :
PRO-1048Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ATG4B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-393 a.a.) and having a molecular mass of 45.4kDa.ATG4B is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATG4B protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cysteine protease ATG4B (ATG4B) belongs to the autophagin protein family. Autophagy is the manner by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is vital for cell homeostasis and cell remodeling during differentiation, metamorphosis, non-apoptotic cell death, and aging. ATG4B is a cysteine protease necessary for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is then transformed to a smaller form (form II). Form II, with an exposed C-terminal glycine, is deemed to be the phosphatidylethanolamine (PE)-conjugated form, and is capable of binding to autophagosomes. Reduced levels of autophagy are seen in some malignant tumors; therefore autophagy may have a role in controlling the unregulated cell growth linked to cancer.
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Synonyms
Cysteine protease ATG4B, AUT-like 1 cysteine endopeptidasem, Autophagin-1, Autophagy-related cysteine endopeptidase 1, Autophagy-related protein 4 homolog B, hAPG4B, ATG4B, APG4B, AUTL1, KIAA0943.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRKNFPA IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFS VLNAFIDRKD SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR RLCRTSVPCA GATAFPADSD RHCNGFPAGA EVTNRPSPWR PLVLLIPLRL GLTDINEAYV ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVEPTD GCFIPDESFH CQHPPCRMSI AELDPSIAVG FFCKTEDDFN DWCQQVKKLS LLGGALPMFE LVEQQPSHLA CPDVLNLSLD SSDVERLERF FDSEDEDFEI LSLLEHHHHH H.
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.