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894 results found for “Density Lipoprotein”
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Name :
BD 4 HumanDescription:
Beta Defensin-4 Human Recombinant
HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.
Product # :
CYT-599Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Beta Defensin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 50 amino acids and having a molecular mass of 6 kDa. The BD-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DEFB4 (1mg/ml) was lyophilized with 20mM sodium Phosphate buffer pH-7.4 and 130mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.More Info
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Introduction
Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues. -
Synonyms
HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Beta Defensin-4 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 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 Beta Defensin-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.
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Background
Beta Defensin-4 Human Recombinant: Exploring the Potential of a Novel Antimicrobial Peptide
Abstract:
Beta Defensin-4 (hBD-4) human recombinant is a promising antimicrobial peptide with unique properties and potential therapeutic applications. This research paper provides an in-depth analysis of hBD-4, including its characteristics, mode of action, and potential uses. Furthermore, novel methodologies for the production and optimization of hBD-4 human recombinant are proposed, shedding light on its future implications in the field of infectious disease management.
Introduction:
In the face of increasing drug-resistant infections, alternative therapeutic strategies are crucial. Antimicrobial peptides, such as hBD-4, have gained attention due to their broad-spectrum activity against pathogens. This paper aims to explore the distinctive features of hBD-4 and propose innovative approaches for its production and optimization.
Characteristics and Mode of Action:
hBD-4 is a cationic peptide comprising 50 amino acids and is characterized by a unique structure that contributes to its antimicrobial properties. The mechanism of action involves the disruption of microbial membranes and subsequent cell death. Additionally, hBD-4 exhibits immunomodulatory effects, including the stimulation of chemotaxis and modulation of the inflammatory response.
Production of hBD-4 Human Recombinant:
Efficient production methodologies for hBD-4 human recombinant are essential for its therapeutic applications. Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents advantages and challenges, necessitating careful selection for high yields and protein quality. Optimization strategies, including codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-4 recombinant.
Potential Applications:
hBD-4 human recombinant demonstrates potential therapeutic applications in combating drug-resistant pathogens. Its broad-spectrum antimicrobial activity against bacteria, viruses, and fungi positions it as a promising candidate for infectious disease management. Moreover, hBD-4 shows promise in wound healing and tissue regeneration due to its ability to promote angiogenesis and stimulate cell migration. Exploring its potential in combination with drug delivery systems for targeted therapy is an exciting avenue for future research.
Conclusion:
hBD-4 human recombinant represents a novel antimicrobial peptide with diverse potential applications. Optimizing production methodologies and elucidating its mechanisms of action will further enhance its clinical utility. With its broad-spectrum antimicrobial activity and potential implications in wound healing and targeted therapy, hBD-4 human recombinant holds promise as an innovative therapeutic agent.
What is the molecular weight/Mw of BD4 Protein?
BD4 Protein has a total Mw of 6kDa.
What is the source or expression system of BD4 Protein?
Escherichia Coli.
What is the Purity of BD4 Protein?
BD4 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD4 Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.
What is the amino acid sequence of BD4 Protein?
EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.
What applications can BD4 Protein be used in?
BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD4 Protein?
The endotoxin level is minimal, BD4 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.
- View Data Sheet
Name :
NDE1 HumanDescription:
nudE Nuclear Distribution Gene E Homolog 1 Human Recombinant
Nuclear distribution protein nudE homolog 1, NudE, NDE1, NUDE, LIS4, NUDE1, HOM-TES-87.
Product # :
PRO-204Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NDE1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (1-335 a.a.) and having a molecular mass of 39.9kDa (Molecular weight on SDS-PAGE will appear higher).NDE1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDE1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 5mM DTT and 0.2M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
NDE1 is a cytoplasmic protein which is a member of the nudE protein family. Phosphorylated during mitosis, NDE1 is critical for the formation and function of the mitotic spindle in M phase and functions to regulate the Dynein-mediated transport of kinetochore proteins, as well as centrosome duplication during interphase. NDE1 is believed to interact with NDEL1, LIS1 and Dynein IC1/2, cytosolic in a signaling pathway which regulates the formation of neurons and is fundamental to the development of the cerebral cortex.
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Synonyms
Nuclear distribution protein nudE homolog 1, NudE, NDE1, NUDE, LIS4, NUDE1, HOM-TES-87.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
NDE1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEDSGKTFSS EEEEANYWKD LAMTYKQRAE NTQEELREFQ EGSREYEAEL ETQLQQIETR NRDLLSENNR LRMELETIKE KFEVQHSEGY RQISALEDDL AQTKAIKDQL QKYIRELEQA NDDLERAKRA TIMSLEDFEQ RLNQAIERNA FLESELDEKE NLLESVQRLK DEARDLRQEL AVQQKQEKPR TPMPSSVEAE RTDTAVQATG SVPSTPIAHR GPSSSLNTPG SFRRGLDDST GGTPLTPAAR ISALNIVGDL LRKVGALESK LASCRNLVYD QSPNRTGGPA SGRSSKNRDG GERRPSSTSV PLGDKGLDTS CRWLSKSTTR SSSSC.
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 :
ARFIP2 HumanDescription:
ADP-Ribosylation Factor Interacting Protein 2 Human Recombinant
ADP-ribosylation factor interacting protein 2, partner of RAC1 (arfaptin 2), Partner of RAC1, Protein POR1, arfaptin-2, POR1.
Product # :
PRO-1201Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARFIP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 364 amino acids (1-341) and having a molecular mass of 40.2 kDa.ARFIP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ARFIP2 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Arfaptin 2 (ARFIP2) is a Rac1 binding protein essential for Rac-mediated actin polymerization and the succeeding formation of membrane ruffles and lamellipodia. ARFIP2 is a putative target protein of ADP-ribosylation factor. ARFIP2 is also involved in membrane ruffling. ARFIP2 expression is increased at sites of neurodegeneration. In addition, ARFIP2 interacts with the ADP ribosylation factor ARF6, a GTPase which associates with the plasma membrane and intracellular endosome vesicles, in a GTP dependent mode. Furthermore, Arfaptin 2 controls the aggregation of mutant Huntingtin protein by weakening proteasome function.
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Synonyms
ADP-ribosylation factor interacting protein 2, partner of RAC1 (arfaptin 2), Partner of RAC1, Protein POR1, arfaptin-2, POR1.
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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 MGS TDGILG KAATMEIPIH GNGEARQLPE DDGLEQDLQQ VMVSGPNLNE TSIVSGGYGG SGDGLIPTGS GRHPSHSTTP SGPGDEVARG IAGEKFDIVK KWGINTYKCT KQLLSERFGR GSRTVDLELE LQIELLRETK RKYESVLQLG RALTAHLYSL LQTQHALGDA FADLSQKSPE LQEEFGYNAE TQKLLCKNGE TLLGAVNFFV SSINTLVTKT MEDTLMTVKQ YEAARLEYDA YRTDLEELSL GPRDAGTRGR LESAQATFQA HRDKYEKLRG DVAIKLKFLE ENKIKVMHKQ LLLFHNAVSA YFAGNQKQLE QTLQQFNIKL RPPGAEKPSW LEEQ
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 :
FABP1 MouseDescription:
Fatty Acid Binding Protein-1 Mouse Recombinant
Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.
Product # :
PRO-1121Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Fatty Acid Binding Protein-1 Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The FABP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.
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Synonyms
Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FABP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FABP1 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 FABP1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY KRVSKRI.
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 :
KDSR HumanDescription:
3-Ketodihydrosphingosine Reductase Human Recombinant
3-ketodihydrosphingosine reductase, KDS reductase, 3-dehydrosphinganine reductase, Follicular variant translocation protein 1, FVT-1, KDSR, FVT1, DHSR, SDR35C1, FLJ36555, FLJ92680.
Product # :
ENZ-092Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KDSR Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 266 amino acids (26-270 a.a.) and having a molecular mass of 29kDa. The KDSR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KDSR solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl and 0.1mM PMSF.
Purity
KDSR purity was found to be greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
3-ketodihydrosphingosine reductase (KDSR) is a 332 amino acid multi-pass membrane protein which localizes to the ER and is a member of the short-chain dehydrogenases/reductases (SDR) family. KDSR is a secreted protein that is weakly expressed in hematopoietic tissue. Furthermore, KDSR catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). The putative active site residues of KDSR are found on the cytosolic side of the endoplasmic reticulum membrane. Chromosomal rearrangement in the KDSR gene is a cause of follicular lymphoma, aka type II chronic lymphatic leukemia.
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Synonyms
3-ketodihydrosphingosine reductase, KDS reductase, 3-dehydrosphinganine reductase, Follicular variant translocation protein 1, FVT-1, KDSR, FVT1, DHSR, SDR35C1, FLJ36555, FLJ92680.
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Physical Appearance
The KDSR is supplied as a 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 MKPLALPGAH VVVTGGSSGI GKCIAIECYK QGAFITLVAR NEDKLLQAKK EIEMHSINDK QVVLCISVDV SQDYNQVENV IKQAQEKLGP VDMLVNCAGM AVSGKFEDLE VSTFERLMSI NYLGSVYPSR AVITTMKERR VGRIVFVSSQ AGQLGLFGFT AYSASKFAIR GLAEALQMEV KPYNVYITVA YPPDTDTPGF AEENRTKPLE TRLISETTSV CKPEQVAKQI VKDAIQGNFN SSLGSD.
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 :
PNOC HumanDescription:
Prepronociceptin Human Recombinant
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
Product # :
PRO-1442Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PNOC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (20-176) and having a molecular mass of 20.6kDa. PNOC is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
PNOC protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.
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Synonyms
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
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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 MGSSCQRDCL TCQEKLHPAL DSFDLEVCIL ECEEKVFPSP LWTPCTKVMA RSSWQLSPAA PEHVAAALYQ PRASEMQHLR RMPRVRSLFQ EQEEPEPGME EAGEMEQKQL QKRFGGFTGA RKSARKLANQ KRFSEFMRQY LVLSMQSSQR RRTLHQNGNV.
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 :
LDOC1L HumanDescription:
Leucine Zipper, Down-Regulated in Cancer 1-Like Human Recombinant
Protein LDOC1L, Leucine zipper protein down-regulated in cancer cells-like, Mammalian retrotransposon-derived protein 6, LDOC1L, MAR6, MART6, dJ1033E15.2.
Product # :
PRO-1153Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LDOC1L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-239 a.a) and having a molecular mass of 28.7kDa.LDOC1L is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LDOC1L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% glycerol, 2mM DTT, 0.1mM PMSF and 1mM EDTA.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Leucine zipper down-regulated in cancer 1-like (LDOC1L) is a member of the LDOC1 family. LDOC1L is a nuclear protein containing a leucine zipper-like motif and a proline-rich region that shares noticeable similarity with an SH3-binding domain. LDOC1L localizes to the nucleus and is downregulated in certain cancer cell lines. LDOC1L is believed to regulate the transcriptional response mediated by the nuclear factor kB (NFkB).
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Synonyms
Protein LDOC1L, Leucine zipper protein down-regulated in cancer cells-like, Mammalian retrotransposon-derived protein 6, LDOC1L, MAR6, MART6, dJ1033E15.2.
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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 MGSHMVQPQT SKAESPALAA SPNAQMDDVI DTLTSLRLTN SALRREASTL RAEKANLTNM LESVMAELTL LRTRARIPGA LQITPPISSI TSNGTRPMTT PPTSLPEPFS GDPGRLAGFL MQMDRFMIFQ ASRFPGEAER VAFLVSRLTG EAEKWAIPHM QPDSPLRNNY QGFLAELRRT YKSPLRHARR AQIRKTSASN RAVRERQMLC RQLASAGTGP CPVHPASNGT SPAPALPARA RNL.
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 :
PRDX3 HumanDescription:
Peroxiredoxin-3 Human Recombinant
AOP1, MER5, AOP-1, SP-22, PRO1748, MGC24293, MGC104387, PRDX3, Thioredoxin-dependent peroxide reductase mitochondrial, Peroxiredoxin-3, PRX III, Antioxidant protein 1, Protein MER5 homolog, HBC189.
Product # :
ENZ-419Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
PRDX3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids (63-256 a.a.) and having a molecular mass of 21.5 kDa.The PRDX3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PRDX3 solution contains 20mM Tris-HCl pH-8, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be approximately 82-83 pmole/min/µg.
The enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX3 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for 1 minute.More Info
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Introduction
PRDX3 is part of the peroxiredoxin family of antioxidant enzymes, that reduces hydrogen peroxide and alkyl hydroperoxides. PRDX3 is particularly located in the mitochondria and involved in the regulation of cellular redox status by serving as a primary line of defense against H2O2 produced during respiration. PRDX3 is a significant regulator of the abundance of mitochondrial H(2)O(2), which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling. PRDX3 mitochondrial protein is significantly decreased in Alzheimer Disease and Down Syndrome.
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Synonyms
AOP1, MER5, AOP-1, SP-22, PRO1748, MGC24293, MGC104387, PRDX3, Thioredoxin-dependent peroxide reductase mitochondrial, Peroxiredoxin-3, PRX III, Antioxidant protein 1, Protein MER5 homolog, HBC189.
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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
MPAVTQHAPY FKGTAVVNGE FKDLSLDDFK GKYLVLFFYP LDFTFVCPTE IVAFSDKANE FHDVNCEVVA VSVDSHFSHL AWINTPRKNG GLGHMNIALL SDLTKQISRD YGVLLEGSGL ALRGLFIIDP NGVIKHLSVN DLPVGRSVEE TLRLVKAFQY VETHGEVCPA NWTPDSPTIK PSPAASKEYF QKVNQ.
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 :
CDNF MouseDescription:
Cerebral Dopamine Neurotrophic Factor Mouse Recombinant
Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.
Product # :
CYT-729Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CDNF Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.More Info
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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for dopamine neurons. CDNF inhibits the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the dopaminergic function and inhibits the degeneration of dopaminergic neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
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Synonyms
Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF 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 CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.
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Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.5kDa.
What is the source or expression system of CDNF Protein?
Escherichia Coli.
What is the Purity of CDNF Protein?
CDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CDNF Protein?
CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.
What is the amino acid sequence of CDNF Protein?
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.
What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF 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.
- View Data Sheet
Name :
CRIP1 HumanDescription:
Cysteine-Rich Protein 1 Human Recombinant
Cysteine-rich protein 1, Cysteine-rich heart protein, CRHP, hCRHP, Cysteine-rich intestinal protein, CRIP, CRP1.
Product # :
PRO-1563Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CRIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77 a.a) and having a molecular mass of 10.9kDa.CRIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRIP1 protein solution (0.25mg/ml) containing 20mM Tris-HCl(pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CRIP1 also known as Cysteine-Rich Protein 1is a member to the LIM/double zinc finger protein family, membersof which comprise cysteine- and glycine-rich protein-1, rhombotin-1, rhombotin-2, and rhombotin-3. CRIP1 may beimplicated in zinc absorption and also may function as an intracellular zinc transport protein. Among the diseases associated with CRIP1 are situs inversus, and osteosarcoma.
-
Synonyms
Cysteine-rich protein 1, Cysteine-rich heart protein, CRHP, hCRHP, Cysteine-rich intestinal protein, CRIP, CRP1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPKCPKC NKEVYFAERV TSLGKDWHRP CLKCEKCGKT LTSGGHAEHE GKPYCNHPCY AAMFGPKGFG RGGAESHTFK
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 :
Borrelia Garinii DbpADescription:
Borrelia Garinii Decorin Binding Protein A Recombinant
Product # :
BOR-025Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Borrelia Garinii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19kDa. Borrelia Garinii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Garinii DbpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. Borreliella garinii DbpA demonstrates the typical lipid anchor and decorin/glycoaminoglycon binding properties of a DbpA protein.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.
-
Applications
Western blot with Lyme positive plasma.
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 :
Borrelia Spielmanii OspCDescription:
Borrelia Spielmanii Outer Surface Protein C Recombinant
Product # :
BOR-009Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Borrelia Spielmanii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 24kDa. Borrelia Spielmanii OspC is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Spielmanii OspC is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).
-
Applications
Western blot with patient sample.
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 :
Avidin ProteinDescription:
Avidin
Avidin, AVD, AVID.
Product # :
PRO-500Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- biological activity
- More Info
Description
Avidin is a glycosylated polypeptide chain having a molecular mass of 68kDa and containing 4 subunits each with a binding site for biotin. The Avidin is purified by affinity chromatographic techniques.The purification procedure ensures minimal contamination by other proteins or DNA.The resulting high activity and purity of the product gives very low non-specific binding (NSB).
Source
Hen's egg white.
Biological Activity
15.0 units/mg protein, 1 unit binds 1µg biotin.
More Info
-
Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of four to five mannose and three N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
-
Synonyms
Avidin, AVD, AVID.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Avidin 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 Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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.
- View Data Sheet
Name :
SPP1 Human, ActiveDescription:
Osteopontin Human Recombinant, BioActive
OPN, SPP-1, BNSP, BSPI, ETA-1, Bone sialoprotein 1, BSP I.Early T lymphocyte activation 1, ETA 1, ETA1, MGC110940, Nephropontin, Secreted phosphoprotein 1, SPP 1, SPP1, urinary stone protein, uropontin.
Product # :
CYT-1166Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
SPP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 321 amino acids (17-314 a.a.) and having a molecular mass of 36.2kDa. SPP1 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 1mM DTT, 10% glycerol and 2mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by the ability of the immobilized protein to support the adhesion of HEK293 human embryonic kidney cells. When cells are added to OPN coated plates 10ug/ml. This effect is more to 40%.
More Info
-
Introduction
Osteopontin is a glycoprotein that was primarilyfound in osteoblasts and takes part in bone remodeling, immune functions in fibroblasts, macrophages, & lymphocytes during inflammation and wound healing. SPP1 highlybinds to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury through late preconditioning. Expression of Ostepontin and CD44 in hepatocellular carcinoma is linked to advanced tumor stage &leads to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases. -
Synonyms
OPN, SPP-1, BNSP, BSPI, ETA-1, Bone sialoprotein 1, BSP I.Early T lymphocyte activation 1, ETA 1, ETA1, MGC110940, Nephropontin, Secreted phosphoprotein 1, SPP 1, SPP1, urinary stone protein, uropontin.
-
Physical Appearance
Sterile Filtered clear 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 RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV N.
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 :
RPL35 HumanDescription:
Ribosomal Protein L35 Human Recombinant
Ribosomal Protein L35, 60S Ribosomal Protein L35, RPL35A, DBA5, L35, 60S ribosomal protein L35.
Product # :
PRO-2097Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RPL35 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (1-123 a.a) and having a molecular mass of 16.9kDa. RPL35 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RPL35 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
Ribosomal Protein L35, also known as RPL35 is a ribosomal protein which is a component of the 60S subunit. Ribosomes are the organelles which catalyze protein synthesis, they consist of a small 40S subunit and a large 60S subunit. Jointly these subunits are composed of 4 RNA species and about 80 structurally different proteins. RPL35 is a member of the L29P family of ribosomal proteins. RPL35 is located in the cytoplasm. As typicaly for genes encoding ribosomal proteins, there are multiple processed pseudogenes of RPL35 dispersed through the genome.
-
Synonyms
Ribosomal Protein L35, 60S Ribosomal Protein L35, RPL35A, DBA5, L35, 60S ribosomal protein L35.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAKIKAR DLRGKKKEEL LKQLDDLKVE LSQLRVAKVT GGAASKLSKI RVVRKSIARV LTVINQTQKE NLRKFYKGKK YKPLDLRPKK TRAMRRRLNK HEENLKTKKQ QRKERLYPLR KYAVKA.
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 :
Dengue Envelope-1 45kDaDescription:
Dengue Virus Subtype 1 Envelope 45kDa Recombinant
Product # :
DEN-021Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Dengue Virus Subtype 1 Envelope 45kDa (43-413a.a.) produced in E.coli, contains important epitopes for dengue antibody recognition. This protein is fused to a 6xHis tag.
Source
E.coli.
Formulation
Phosphate buffered saline with 25mM arginine.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
-
Introduction
Dengue fever is affected by 1 of 4 closely linked virus serotypes of the genus Flavivirus, family Flaviviridae. One might have dengue fever infected by the different serotype virus after the primary infection. Detection of particular antibodies to dengue viruses is used for the diagnosis in clinic. Recently, lateral flow rapid test products have become a most suitable and known method in the clinical diagnosis. Though, there is difficulty for manufacturers to have the dengue antigens with a whole coverage for Dengue IgG & IgM recognition for all 4 serotype infections as well as with colloid gold binding ability. 8 dengue antigens have been established for the lateral flow products which are well defined for their coverage of dengue IgG & IgM recognition. The researcher can select the products below based on their own specific application.
-
Stability
Dengue Envelope-1 45kDa although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
Can be used for lateral flow & ELISA assay.
-
Purification Method
Purified by proprietary chromatographic technique
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Dengue Envelope-3 45kDaDescription:
Dengue Virus Subtype 3 Envelope 45kDa Recombinant
Product # :
DEN-023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Dengue Virus Subtype 3 Envelope 45kDa (a.a 43-413) is produced in E.coli. This protein is fused to 6xHis tag at C-terminus.
Source
E.coli.
Formulation
25mM Tris base and 10mM K2CO3.
Purity
Protein is >95% pure as determined by 10% SDS-PAGE (coomassie staining).
More Info
-
Introduction
Dengue fever is affected by 1 of 4 closely linked virus serotypes of the genus Flavivirus, family Flaviviridae. One might have dengue fever infected by the different serotype virus after the primary infection. Detection of particular antibodies to dengue viruses is used for the diagnosis in clinic. Recently, lateral flow rapid test products have become a most suitable and known method in the clinical diagnosis. Though, there is difficulty for manufacturers to have the dengue antigens with a whole coverage for Dengue IgG & IgM recognition for all 4 serotype infections as well as with colloid gold binding ability. 8 dengue antigens have been established for the lateral flow products which are well defined for their coverage of dengue IgG & IgM recognition. The researcher can select the products below based on their own specific application.
-
Stability
Dengue Envelope-3 45kDa although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
Immunoassay.
-
Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LLO PEST freeDescription:
Listeriolysin-O PEST free Recombinant
Listeriolysin-O, LLO, hlyA.
Product # :
PRO-373Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Recombinant Listeriolysin O s a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. PEST sequence is 19 amino acids peptide located at the protein NH 2-terminus, that targets the toxin for degradation. This motif is essential for bacterial virulence.
Source
Escherichia Coli.
Formulation
The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol and 0.5M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
7x104 HU/mg. 2mM DTT could be use to reactivate the toxin.
More Info
-
Introduction
Listeriolysin O (aka LLO) is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents and inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes (average pH ~ 5.9) of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, and the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system and antibodies. LLO also brings about dephosphorylation of histone H3 and deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO and is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST's supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO.
-
Synonyms
Listeriolysin-O, LLO, hlyA.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin DogDescription:
Leptin Dog Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-506Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Dog Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
-
Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
-
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Dengue Envelope-2 22kDaDescription:
Dengue Virus Subtype-2 Envelope 22kDa Recombinant
Product # :
DEN-007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
The E.coli derived recombinant 22 kDa protein is genetically engineered peptide which is derived from Dengue Type-2 Envelope. This region also contains a common antigen for Dengue IgG & IgM. This protein is fused to 6xHis tag.
Source
Escherichia Coli.
Formulation
Phosphorous buffered saline, pH-7.4.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
-
Introduction
Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.
-
Stability
Dengue Envelope ST2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
Each laboratory should determine an optimum working titer for use in its particular application.
-
Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Dengue Envelope-2 32kDaDescription:
Dengue Virus Subtype 2 Envelope 32kDa Recombinant
Product # :
DEN-018Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Dengue Virus Subtype 2 Envelope 32kDa, produced in E.coli, amino acids 45-297 and fused to a 6xHis Tag, containing domains I+II of the dengue envelope.
Source
E.coli.
Formulation
Phosphate buffer.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
-
Introduction
Dengue fever is affected by 1 of 4 closely linked virus serotypes of the genus Flavivirus, family Flaviviridae. One might have dengue fever infected by the different serotype virus after the primary infection. Detection of particular antibodies to dengue viruses is used for the diagnosis in clinic. Recently, lateral flow rapid test products have become a most suitable and known method in the clinical diagnosis. Though, there is difficulty for manufacturers to have the dengue antigens with a whole coverage for Dengue IgG & IgM recognition for all 4 serotype infections as well as with colloid gold binding ability. 8 dengue antigens have been established for the lateral flow products which are well defined for their coverage of dengue IgG & IgM recognition. The researcher can select the products below based on their own specific application.
-
Stability
Dengue Envelope-2 32kDa although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
Can be used for immunoassay.
-
Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CST3 Protein, HisDescription:
Cystatin-C Human Recombinant, His Tag
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Product # :
PRO-656Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
-
Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
-
Synonyms
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. 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
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 in the cell culture.
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 :
PDI HumanDescription:
Protein Disulfide Isomerase Human Recombinant
Protein Disulfide Isomerase, PDI, EC 5.3.4.1, Prolyl 4-hydroxylase subunit beta, Cellular thyroid hormone-binding protein, p55, P4HB, ERBA2L, PDIA1, PO4DB, DSI, GIT, PHDB, PO4HB, PROHB, P4Hbeta.
Product # :
ENZ-262Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
PDI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 502 amino acids and having a molecular mass of 56.6kDa. The PDI is fused to a 12 amino acid His tag at N-terminal and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PDI protein (1mg/ml)solution was lyophilized from PBS pH-7.
Purity
Greater than 95.0% as determined by:
a) Analysis by RP-HPLC.
b) Analysis by SDS-PAGE.More Info
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Introduction
Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. -
Synonyms
Protein Disulfide Isomerase, PDI, EC 5.3.4.1, Prolyl 4-hydroxylase subunit beta, Cellular thyroid hormone-binding protein, p55, P4HB, ERBA2L, PDIA1, PO4DB, DSI, GIT, PHDB, PO4HB, PROHB, P4Hbeta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein Disulfide Isomerase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human PDI 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 avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PDI in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MRGSGSHHHHHHAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKA
AGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVN
WLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNS
DVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIK
THILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITL
EEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEK
KNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFP
ASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
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Reductase Activity
0.001 650nm/ min-2. By measuring the turbidity increase at 650 nm due to insulin reduction (Holmgren, A. (1979) J. Biol. Chem. 254, 9627–9632). The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time (Mart
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Isomerase Activity
0.5 µmol active RNase A min-1 µmol PDI-1. According to the re-activation of reduced and denatured RNase A (Lyles, M. M. and Gilbert, H. F. (1991) Biochemistry 30, 613-619).
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 :
GDF3 HumanDescription:
Growth Differentiation Factor-3 Human Recombinant
Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.
Product # :
CYT-694Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated solution (0.5mg/ml) containing 30mM Acetate buffer pH-4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.
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Synonyms
Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF3 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 GDF3 in sterile 100mM Acetate buffer pH-4 at a concentration of 0.5mg/ml. For the dilution into higher pH values, it is recommended to dilute the protein to a concentration of 10μg/ml. Please note that in higher concentrations the solubility of GDF3 is limited. The protein is not sterile! Please sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.
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Background
What is the molecular weight/Mw of GDF3 HUMAN Protein?
GDF3 HUMAN Protein has a total Mw of 14.15XkDa.
What is the source or expression system of GDF3 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF3 HUMAN Protein?
GDF3 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF3 HUMAN Protein?
The biological functionality of GDF3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF3 HUMAN Protein?
MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.
What applications can GDF3 HUMAN Protein be used in?
GDF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF3 HUMAN Protein?
The endotoxin level is minimal, GDF3 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.