Search: 1000 results found for "Dickkopf-Related Protein"

Description:

SLAMF7 Human Recombinant

SLAMF7, SLAM Family Member 7, CD2-Like Receptor-Activating Cytotoxic Cells, Membrane Protein FOAP-12, CD2 Subset 1, Protein 19A, CRACC, CS1, Novel LY9 (Lymphocyte Antigen 9) Like Protein, CD2-Like Receptor Activating Cytotoxic Cells, 19A24 Protein, CD319 Antigen, Novel Ly9, CD319, 19A.

Product # :

PRO-2261

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Description

SLAMF7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 212 amino acids (23-226a.a.) and having a molecular mass of 23.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). SLAMF7 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SLAMF7 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.

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Introduction
SLAMF7 belongs to the CS2 family of cell surface receptors. SLAMF7 is a single-pass type 1 membrane protein, SLAMF7 Isoform 1 mediates NK cell activation via aSH2D1A-independent extracellular signal-regulated ERK-mediated pathway. SLAMF7 functions in lymphocyteadhesion. Furthermore, SLAMF7 can exert activating of inhibitory influences on cells of the immune system depending on cellular context as well as the availability of effector proteins.
Synonyms
SLAMF7, SLAM Family Member 7, CD2-Like Receptor-Activating Cytotoxic Cells, Membrane Protein FOAP-12, CD2 Subset 1, Protein 19A, CRACC, CS1, Novel LY9 (Lymphocyte Antigen 9) Like Protein, CD2-Like Receptor Activating Cytotoxic Cells, 19A24 Protein, CD319 Antigen, Novel Ly9, CD319, 19A.
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
SGPVKELVGS VGGAVTFPLK SKVKQVDSIV WTFNTTPLVT IQPEGGTIIV TQNRNRERVD FPDGGYSLKL SKLKKNDSGI YYVGIYSSSL QQPSTQEYVL HVYEHLSKPK VTMGLQSNKN GTCVTNLTCC MEHGEEDVIY TWKALGQAAN ESHNGSILPI SWRWGESDMT FICVARNPVS RNFSSPILAR KLCEGAADDP DSSMLEHHHH 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.

Description:

Microfibrillar-associated Protein 2 Human Recombinant

Microfibrillar-associated protein 2, MFAP-2, Microfibril-associated glycoprotein 1, MAGP, MAGP-1, MFAP2, MAGP1.

Product # :

PRO-1265

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Description

MFAP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (18-183 a.a) and having a molecular mass of 21.5kDa.MFAP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MFAP2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Microfibrillar-associated protein 2 (MFAP2) is an O-glycosylated protein discharged to the extracellular space and the extracellular matrix. MFAP2 connects with biglycan and elastin in a ternary complex. MFAP2 plays a key role in the support and distensibility of the juxtacanalicular region of these collector channels. MFAP2 inhibits LTB-1 binding to fibrillin-1, promotes the phosphorylation of Smad2 thus mediating the consequent extracellular deposition of latent TGFbeta.
Synonyms
Microfibrillar-associated protein 2, MFAP-2, Microfibril-associated glycoprotein 1, MAGP, MAGP-1, MFAP2, MAGP1.
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 MGSMQGQYDL DPLPPFPDHV QYTHYSDQID NPDYYDYQEV TPRPSEEQFQ FQSQQQVQQE VIPAPTPEPG NAELEPTEPG PLDCREEQYP CTRLYSIHRP CKQCLNEVCF YSLRRVYVIN KEICVRTVCA HEELLRADLC RDKFSKCGVM ASSGLCQSVA ASCARSCGSC.

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

Description:

ADP-Ribosylation Factor Interacting Protein 1 341 a.a Human Recombinant

HSU52521, ADP-ribosylation factor-interacting protein 1, Arfaptin-1.

Product # :

PRO-2089

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Description

ARFIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-341 a.a) and having a molecular mass of 41.0kDa.ARFIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ARFIP1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ADP-Ribosylation Factor Interacting Protein 1 (ARFIP1) contains 1 AH domain and is a putative target protein of ADP-ribosylation factor.
Synonyms
HSU52521, ADP-ribosylation factor-interacting protein 1, Arfaptin-1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQESPK NSAAEIPVTS NGEVDDSREH SFNRDLKHSL PSGLGLSETQ ITSHGFDNTK EGVIEAGAFQ GGQRTQTKSG PVILADEIKN PAMEKLELVR KWSLNTYKCT RQIISEKLGR GSRTVDLELE AQIDILRDNK KKYENILKLA QTLSTQLFQM VHTQRQLGDA FADLSLKSLE LHEEFGYNAD TQKLLAKNGE TLLGAINFFI ASVNTLVNKT IEDTLMTVKQ YESARIEYDA YRTDLEELNL GPRDANTLPK IEQSQHLFQA HKEKYDKMRN DVSVKLKFLE ENKVKVLHNQ LVLFHNAIAA YFAGNQKQLE QTLKQFHIKL KTPGVDAPSW 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.

Description:

Granulocyte-Colony Stimulating Factor Rat Recombinant

Granulocyte colony stimulating factor, Protein Csf3, Csf3.

Product # :

CYT-940

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Description

GCSF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.5kDa.The G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in 5mM Sodium Citrate, pH 4.0.

Purity

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

Biological Activity

The ED₅₀ determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 10⁷ IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
Granulocyte colony stimulating factor, Protein Csf3, Csf3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF 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 GCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.
Background
What is the molecular weight/Mw of G CSF RAT Protein?
G CSF RAT Protein has a total Mw of 21.5kDa.

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

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

What is the Biological Activity of G CSF RAT Protein?
The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

What is the amino acid sequence of G CSF RAT Protein?
KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

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

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

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

Description:

Nephroblastoma Overexpressed Human Recombinant

Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

Product # :

CYT-805

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Description

Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.

Purity

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

Biological Activity

Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

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Introduction
Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NOV although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NOV 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 NOV in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK 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.

Description:

Precursor Brain-Derived Neurotrophic Factor Human Recombinant

proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

Product # :

CYT-014

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

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Introduction
proBDNF (the precursor form of Brain-derived neurotrophic factor) interacts preferentially with p75NTR (the pan-neurotrophin receptor p75) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, while the mature BDNF selectively binds with great affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. Since proneurotrophins and mature neurotrophins bring forth opposite biological effects, proBDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. proBDNF has an important role in negative regulation of neurotrophic actions in the brain.
Synonyms
proBDNF, Precursor Form Brain-derived Neurotrophic Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized proBDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution proBDNF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized proBDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.
Background
Precursor Brain-Derived Neurotrophic Factor Human Recombinant: Unveiling the Potential of a Key Neurotrophic Factor
Abstract:
Precursor Brain-Derived Neurotrophic Factor (proBDNF) human recombinant is a pivotal neurotrophic factor that plays a critical role in neuronal development, survival, and synaptic plasticity. This research paper provides a comprehensive overview of proBDNF, including its characteristics, processing mechanisms, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of proBDNF human recombinant are proposed, highlighting its future implications in the field of neuroregenerative medicine.
Introduction:
Understanding the intricate processes underlying neuronal development and function is crucial for advancing neuroregenerative strategies. Neurotrophic factors, such as proBDNF, have garnered significant attention due to their pivotal roles in supporting neuronal growth and survival. This paper delves into the unique features of proBDNF and presents novel approaches for its production and optimization.
Characteristics and Processing Mechanisms:
proBDNF is a precursor protein consisting of 247 amino acids and is processed into mature brain-derived neurotrophic factor (mBDNF) through proteolytic cleavage. The ratio between proBDNF and mBDNF is tightly regulated and determines the balance between neuronal survival and apoptosis. Additionally, proBDNF exerts distinct biological functions through its receptor interactions, modulating synaptic plasticity and neuronal activity.
Production of proBDNF Human Recombinant:
Efficient production methodologies are essential to harness the therapeutic potential of proBDNF human recombinant. Various expression systems, including bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents unique advantages and challenges, necessitating careful selection to achieve high yields and protein quality. Optimization strategies, such as codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality proBDNF recombinant.
Potential Therapeutic Applications:
proBDNF human recombinant holds immense promise for neuroregenerative medicine. Its role in promoting neuronal survival, axonal growth, and synaptic plasticity positions it as a valuable therapeutic agent for neurodegenerative disorders, spinal cord injuries, and stroke. Additionally, the balance between proBDNF and mBDNF presents a potential therapeutic target for fine-tuning neuronal processes and restoring proper brain function.
Conclusion:
proBDNF human recombinant represents a crucial neurotrophic factor with diverse therapeutic applications in neuroregenerative medicine. Optimizing production methodologies and further understanding its processing mechanisms will enhance its clinical utility. With its potential implications in neurodegenerative disorders and neuronal repair, proBDNF human recombinant holds immense promise as a transformative tool for promoting neural health and regeneration.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 52kDa.

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

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

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

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

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

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

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

Description:

Nuclear Import 7 Homolog Human Recombinant

Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.

Product # :

PRO-780

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Description

NIP7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-180 a.a.) and having a molecular mass of 21.5kDa. NIP7 is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NIP7 protein solution contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
60S ribosome subunit biogenesis protein NIP7 homolog (NIP7) belongs to NIP7 family and contains 1 PUA domain. NIP7 interacts with pre-ribosome complex and may bind to RNA. NIP7 is vital for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Synonyms
Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRPLTEEETR VMFEKIAKYI GENLQLLVDR PDGTYCFRLH NDRVYYVSEK IMKLAANISG DKLVSLGTCFGKFTKTHKFR LHVTALDYLA PYAKYKVWIK PGAEQSFLYG NHVLKSGLGR ITENTSQYQG VVVYSMADIPLGFGVAAKST QDCRKVDPMA IVVFHQADIG EYVRHEETLT LEHHHHHH.

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

Description:

Stress-Induced-Phosphoprotein 1 Human Recombinant, His Tag

HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.

Product # :

PRO-753

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Description

Recombinant Human STIP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543 a.a) and having a molecular mass of 64.8kDa. STIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

The STIP1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA, 0.2mM PMSF and 20% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.
Synonyms
HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPDWGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLRNKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDKAKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH TPDVLKKCQQAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC QLEPTFIKGYTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.

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

Description:

Microtubule-Associated Protein Tau 383 a.a. Human Recombinant

Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

Product # :

PRO-012

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Description

MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MAPT solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain.
Synonyms
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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).Please prevent freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.

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

Description:

ADP-Ribosylation Factor Interacting Protein 1 Human Recombinant

HSU52521, Arfaptin-1, ADP-ribosylation factor-interacting protein 1.

Product # :

PRO-2088

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Description

ARFIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373 a.a) and having a molecular mass of 44.1kDa.ARFIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ARFIP1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ADP-Ribosylation Factor Interacting Protein 1 (ARFIP1) contains 1 AH domain and is a putative target protein of ADP-ribosylation factor.
Synonyms
HSU52521, Arfaptin-1, ADP-ribosylation factor-interacting protein 1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQESPK NSAAEIPVTS NGEVDDSREH SFNRDLKHSL PSGLGLSETQ ITSHGFDNTK EGVIEAGAFQ GSPAPPLPSV MSPSRVAASR LAQQGSDLIV PAGGQRTQTK SGPVILADEI KNPAMEKLEL VRKWSLNTYK CTRQIISEKL GRGSRTVDLE LEAQIDILRD NKKKYENILK LAQTLSTQLF QMVHTQRQLG DAFADLSLKS LELHEEFGYN ADTQKLLAKN GETLLGAINF FIASVNTLVN KTIEDTLMTV KQYESARIEY DAYRTDLEEL NLGPRDANTL PKIEQSQHLF QAHKEKYDKM RNDVSVKLKF LEENKVKVLH NQLVLFHNAI AAYFAGNQKQ LEQTLKQFHI KLKTPGVDAP SWLEEQ.

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

Description:

Ring Finger Protein 34 Human Recombinant

Ring Finger Protein 34, E3 Ubiquitin Protein Ligase, RING Finger Protein 34, Caspase Regulator CARP1, Caspases-8 And -10-Associated RING Finger Protein 1, FYVE-RING Finger Protein Momo, Human RING Finger Homologous To Inhibitor Of Apoptosis Protein, CARP-1, hRFI, RING Finger Protein RIFF, RFI, CARP1, RIF, RIFF, E3 Ubiquitin-Protein Ligase RNF34, EC 6.3.2.

Product # :

PRO-1761

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Description

RNF34 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.2kDa.RNF34 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RNF34 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Ring Finger Protein 34 (RNF34) has E3 ubiquitin-protein ligase activity. RNF34 has a RINF finger, a motif recognized to be involved in protein-protein and protein-DNA interactions. RNF34 regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. In addition, RNF34 protects cells against apoptosis induced by TNF. RNF34 also binds phosphatidylinositol 5-phosphateand phosphatidylinositol 3-phosphate. Alternatively splicing results in multiple transcript variants encoding distinct isoforms.
Synonyms
Ring Finger Protein 34, E3 Ubiquitin Protein Ligase, RING Finger Protein 34, Caspase Regulator CARP1, Caspases-8 And -10-Associated RING Finger Protein 1, FYVE-RING Finger Protein Momo, Human RING Finger Homologous To Inhibitor Of Apoptosis Protein, CARP-1, hRFI, RING Finger Protein RIFF, RFI, CARP1, RIF, RIFF, E3 Ubiquitin-Protein Ligase RNF34, EC 6.3.2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGS MRKAGAT SMWASCCGLL NEVMGTGAVR GQQSAFAGAT GPFRFTPNPE FSTYPPAATE GPNIVCKACG LSFSVFRKKH VCCDCKKDFC SVCSVLQENL RRCSTCHLLQ ETAFQRPQLM RLKVKDLRQY LILRNIPIDT CREKEDLVDL VLCHHGLGSE DDMDTSSLNS SRSQTSSFFT RSFFSNYTAP SATMSSFQGE LMDGDQTSRS GVPAQVQSEI TSANTEDDDD DDDEDDDDEE ENAEDRNPGL SKERVRASLS DLSSLDDVEG MSVRQLKEIL ARNFVNYSGC CEKWELVEKV NRLYKENEEN QKSYGERLQL QDEEDDSLCR ICMDAVIDCV LLECGHMVTC TKCGKRMSEC PICRQYVVRA VHVFKS

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

Description:

Peroxisomal Biogenesis Factor 19 Human Recombinant

Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.

Product # :

PRO-925

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Description

PEX19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 34.6 kDa.The PEX19 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PEX19 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
PEX19 is vital for peroxisome biogenesis in Saccharomyces cerevisiae. PEX19 is limited to the outer surface of peroxisomes in liver cells and is has a part in the early stage of peroxisome membrane assembly, prior to the import of matrix protein.
Synonyms
Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQC

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

Description:

COP9 Constitutive Photomorphogenic 6 Human Recombinant

CSN6, MOV34-34KD, COP9 signalosome complex subunit 6, JAB1-containing signalosome subunit 6, MOV34 homolog, Vpr-interacting protein, hVIP, COPS6.

Product # :

PRO-1650

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Description

COPS6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 347 amino acids (1-327 a.a.) and having a molecular mass of 38.9kDa.COPS6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

COPS6 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
COP9 Constitutive Photomorphogenic 6 (COPS6) is a member of the translation initiation factor 3 (eIF3) superfamily,peptidase M67A family and CSN6 subfamily. COPS6 is one of 8 subunits of COP9 signalosome,a highly conserved protein complex which functions as an significant regulator in multiple signaling pathways. COP9's structure and function of signalosome is similar to 19S regulatory particle of 26S proteasome. COP9 signalosome can interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases.COP9 takes part in the regulation of cell cycle and likely to be a cellular cofactor for HIV-1 accessory gene product Vpr.
Synonyms
CSN6, MOV34-34KD, COP9 signalosome complex subunit 6, JAB1-containing signalosome subunit 6, MOV34 homolog, Vpr-interacting protein, hVIP, COPS6.
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 MAAAAAAAAA TNGTGGSSGM EVDAAVVPSV MACGVTGSVS VALHPLVILN ISDHWIRMRS QEGRPVQVIG ALIGKQEGRN IEVMNSFELL SHTVEEKIII DKEYYYTKEE QFKQVFKELE FLGWYTTGGP PDPSDIHVHK QVCEIIESPL FLKLNPMTKH TDLPVSVFES VIDIINGEAT MLFAELTYTL ATEEAERIGV DHVARMTATG SGENSTVAEH LIAQHSAIKM LHSRVKLILE YVKASEAGEV PFNHEILREA YALCHCLPVL STDKFKTDFY DQCNDVGLMA YLGTITKTCN TMNQFVNKFN VLYDRQGIGR RMRGLFF.

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

Description:

Adiponectin Human Recombinant, Sf9

Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

Product # :

CYT-1002

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Description

Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Acrp30 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.

sds-page

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Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.
Synonyms
Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding 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. 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
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.9kDa.

What is the source or expression system of ADIPONECTIN Protein?
Sf9, Baculovirus cells.

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

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

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

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

Description:

Growth and Differentiation Factor 15 D-Variant Human Recombinant

GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

Product # :

CYT-314

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Description

GDF15 D-variant (His substitutes Asp at position 7) Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.5kDa. The GDF15 D-variant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF15 D-variant is lyophilized without additives.

Purity

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

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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF15 D-variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 D-variant in sterile 5mM AcOH (acetic Acid) at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MARNGDDCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
Background
What is the molecular weight/Mw of GDF15 D HUMAN Protein?
GDF15 D HUMAN Protein has a total Mw of 24.5kDa.

What is the source or expression system of GDF15 D HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF15 D HUMAN Protein?
GDF15 D HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 D HUMAN Protein?
The biological functionality of GDF15 D HUMAN Protein will be determined in the future.

What is the amino acid sequence of GDF15 D HUMAN Protein?
MARNGDDCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

What applications can GDF15 D HUMAN Protein be used in?
GDF15 D HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF15 D HUMAN Protein?
The endotoxin level is minimal, GDF15 D HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Gastrokine 1 Human Recombinant

BRICHOS domain containing 1, 18 kDa antrum mucosa protein, gastrokine 1, Protein CA11, AMP-18, BRICD1, foveolin, FOV.

Product # :

PRO-1206

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Description

GKN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 223 amino acids (1-199) and having a molecular mass of 24.5 kDa.GKN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GKN1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Gastrokine-1 (GKN1) is a member of the gastrokine family. GKN1 has mitogenic activity and is involved in preserving the integrity of the gastric mucosal epithelium. GKN1 is down-regulated in human gastric cancer tissue in comparison to normal gastric mucosa. GKN1 is expressed in the stomach; however no expression is detected in cancer tissue or gastric cancer cell lines.
Synonyms
BRICHOS domain containing 1, 18 kDa antrum mucosa protein, gastrokine 1, Protein CA11, AMP-18, BRICD1, foveolin, FOV.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSH MLAYSS VHCFREDKMK FTIVFAGLLG VFLAPALANY NINVNDDNNN AGSGQQSVSV NNEHNVANVD NNNGWDSWNS IWDYGNGFAA TRLFQKKTCI VHKMNKEVMP SIQSLDALVK EKKLQGKGPG GPPPKGLMYS VNPNKVDDLS KFGKNIANMC RGIPTYMAEE MQEASLFFYS GTCYTTSVLW IVDISFCGDT VEN.

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

Description:

Autophagy Related 5 Human Recombinant

Autophagy protein 5, APG5-like, Apoptosis-specific protein, ATG5, ASP, APG5, APG5L, hAPG5.

Product # :

PRO-454

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Description

ATG5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-275a.a.) and having a molecular mass of 34.6kDa.ATG5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ATG5 at a concentration of 0.25mg/ml containing 20mM Tris-HCl, pH 8.0, 1mM DTT , 0.2M NaCl and 40% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
ATG5 is a member of the autophagy-related (ATG) genes family. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. ATG5 protein is essential for autophagy. It conjugates to ATG12 and associates with isolation membrane to form autophagosomes. In addition ATG5 takes a vital part in the apoptotic process and it is expressed relatively late in the apoptotic process, downstream of caspase activity.
Synonyms
Autophagy protein 5, APG5-like, Apoptosis-specific protein, ATG5, ASP, APG5, APG5L, hAPG5.
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 MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLPRVSYLTLVTD KVKKHFQKVM RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNITVHFKSFPEK DLLHCPSKDA IEAHFMSCMK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPAEEN GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLKEVCPSAIDPE DGEKKNQVMI HGIEPMLETP LQWLSEHLSY PDNFLHISII PQPTD

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

Description:

Valosin Containing Protein Lysine Methyltransferase Human Recombinant

Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .

Product # :

PRO-2145

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Description

VCPKMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229 a.a.) and having a molecular mass of 28.2kDa.VCPKMT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

VCPKMT protein solution (1mg/ml) containing 20mM Phosphate buffer saline (pH 8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
VCPKMT is a member of the methyltransferase superfamily. VCPKMT is a protein-lysine N-methyltransferase which specifically trimethylates 'Lys-315' of VCP/p97; this alteration reduces VCP ATPase activity.
Synonyms
Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADTLES SLEDPLRSFV RVLEKRDGTV LRLQQYSSGG VGCVVWDAAI VLSKYLETPE FSGDGAHALS RRSVLELGSG TGAVGLMAAT LGADVVVTDL EELQDLLKMN INMNKHLVTG SVQAKVLKWG EEIEGFPSPP DFILMADCIY YEESLEPLLK TLKDISGFET CIICCYEQRT MGKNPEIEKK YFELLQLDFD FEKIPLEKHD EEYRSEDIHI IYIRKKKSKF PS

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

Description:

DnaJ (Hsp40) homolog, subfamily B, member 2 Human Recombinant

DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3.

Product # :

HSP-035

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Description

DNAJB2 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 300 amino acids (1-277 a.a.) and having a molecular mass of 33kDa. The DNAJB2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DNAJB2 solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
DnaJB2 is a member of the DnaJ family. The DnaJ family is one of the largest of all the chaperone families which has evolved with diverse cellular localization and functions. DnaJB2 are important mediators of proteolysis which are involved in the regulation of protein degradation, exocytosis and endocytosis. The DnaJ proteins play a significant role in the HSP70 chaperone machine by interacting with HSP70 to stimulate ATP hydrolysis. DnaJB2 is expressed almost solely in the brain, with the highest levels in the frontal cortex and hippocampus.
Synonyms
DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASYYEI LDVPRSASAD DIKKAYRRKA LQWHPDKNPD NKEFAEKKFK EVAEAYEVLS DKHKREIYDR YGREGLTGTG TGPSRAEAGS GGPGFTFTFR SPEEVFREFF GSGDPFAELF DDLGPFSELQ NRGSRHSGPF FTFSSSFPGH SDFSSSSFSF SPGAGAFRSV STSTTFVQGR RITTRRIMEN GQERVEVEED GQLKSVTING VPDDLALGLE LSRREQQPSV TSRSGGTQVQ QTPASCPLDS DLSEDEDLQL AMAYSLSEME AAGKKPADVF.

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Description:

Complement Factor Properdin Human Recombinant

Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, PROPERDIN.

Product # :

PRO-2011

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Description

CFP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (28-469 a.a.) and having a molecular mass of 50.9kDa.CFP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Complement Factor Properdin (CFP) which is a plasma glycoprotein, is a positive regulator of the alternative complement pathway of the innate immune system. CFP binds and stabilizes the C3- and C5-convertase enzyme complexes in a feedback loop that eventually ends with formation of the membrane attack complex and lysis of the target cell. Mutations in CFP lead to 2 forms of properdin deficiency that cause high susceptibility to meningococcal infections.
Synonyms
Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, PROPERDIN.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDPVLCFT QYEESSGKCK GLLGGGVSVE DCCLNTAFAY QKRSGGLCQP CRSPRWSLWS TWAPCSVTCS EGSQLRYRRC VGWNGQCSGK VAPGTLEWQL QACEDQQCCP EMGGWSGWGP WEPCSVTCSK GTRTRRRACN HPAPKCGGHC PGQAQESEAC DTQQVCPTHG AWATWGPWTP CSASCHGGPH EPKETRSRKC SAPEPSQKPP GKPCPGLAYE QRRCTGLPPC PVAGGWGPWG PVSPCPVTCG LGQTMEQRTC NHPVPQHGGP FCAGDATRTH ICNTAVPCPV DGEWDSWGEW SPCIRRNMKS ISCQEIPGQQ SRGRTCRGRK FDGHRCAGQQ QDIRHCYSIQ HCPLKGSWSE WSTWGLCMPP CGPNPTRARQ RLCTPLLPKY PPTVSMVEGQ GEKNVTFWGR PLPRCEELQG QKLVVEEKRP CLHVPACKDP EEEEL.

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Description:

Polyadenylate-Binding Protein-Interacting protein 2 Human Recombinant

Poly(A) Binding Protein Interacting Protein 2, PABP- interacting protein 2, HSPC218, PAIP-2, PAIP2A, Polyadenylate-binding protein-interacting protein 2, PAIP2, MGC72018.

Product # :

PRO-748

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Description

Recombinant Human PAIP2 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 147 amino acids (1-127 a.a.) and having a molecular mass of 17.1 kDa.PAIP2 human recombinant is fused to 20 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.

Source

Escherichia Coli.

Formulation

The PAIP2 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
PAIP2 has a role as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. PAIP2 inhibitory activity on translation is mediated through its action on PABPC1. PAIP2 displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. PAIP2 association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization.
Synonyms
Poly(A) Binding Protein Interacting Protein 2, PABP- interacting protein 2, HSPC218, PAIP-2, PAIP2A, Polyadenylate-binding protein-interacting protein 2, PAIP2, MGC72018.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKDPSRSSTS PSIINEDVII NGHSHEDDNP FAEYMWMENE EEFNRQIEEE LWEEEFIERC FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDGS SLEDLVVKSN LNPNAKEFVP GVKYGNI.

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Description:

D-Dimer Human

Product # :

PRO-2795

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Description

D-Dimer Human produced in Human Plasma is a specific degradation product of cross-linked fibrin and is used as a marker of hypercoagulation state that causes cardio-vascular diseases. D-Dimer is purified by proprietary chromatographic technique.

Source

Human plasma.

Formulation

D-Dimer was lyophilized from 10mM Tris-HCl and 0.15M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized D-Dimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution D-Dimer 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 D-Dimer in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
D-dimer, a small protein fragment present in the blood after a blood clot dissolves, is a vital marker in the realms of hematology and vascular medicine. Its presence signifies the ongoing process of fibrinolysis, where clots formed in blood vessels are broken down. Beyond its diagnostic significance, understanding the roles of D-dimer in human physiology and pathology is essential for comprehending coagulation disorders and cardiovascular diseases. This research delves into the multifaceted aspects of D-dimer, exploring its physiological functions, diagnostic applications, and implications in various medical conditions.
Physiological Functions:
In physiological conditions, coagulation and fibrinolysis are finely regulated processes, ensuring hemostasis and preventing excessive bleeding or clot formation. D-dimer is a natural byproduct of fibrinolysis, created when plasmin, an enzyme, breaks down fibrin clots. In this context, D-dimer acts as a marker of the body's intricate balance between clot formation and dissolution. It reflects the ongoing maintenance of vascular integrity, showcasing the body's ability to prevent unnecessary clotting.
Diagnostic Significance:
D-dimer holds significant diagnostic value, especially in the context of thrombotic disorders. Elevated levels of D-dimer in the blood are indicative of increased fibrinolysis, potentially signaling an underlying clotting disorder. Clinically, D-dimer assays are widely used to rule out thromboembolic events, such as deep vein thrombosis (DVT) or pulmonary embolism (PE). Moreover, D-dimer levels are crucial in risk stratification and decision-making processes in emergency departments, aiding in the timely diagnosis and treatment of thrombotic conditions.
Cardiovascular Implications:
Research has indicated a strong correlation between elevated D-dimer levels and cardiovascular diseases. In conditions like coronary artery disease (CAD) and stroke, where abnormal clot formation contributes to pathogenesis, D-dimer serves as a prognostic marker. Its presence hints at the ongoing vascular damage and the potential risk of acute events. Studying these correlations provides valuable insights into the progression of cardiovascular diseases, aiding in the development of targeted therapeutic strategies.
Beyond Coagulation Disorders:
Interestingly, recent research has begun to explore D-dimer's involvement in conditions beyond coagulation disorders. Studies suggest links between elevated D-dimer levels and inflammatory diseases, such as sepsis and rheumatoid arthritis. This expanding scope highlights the intricate interplay between coagulation, inflammation, and immune responses, shedding light on novel avenues for therapeutic interventions.
Conclusion:
D-dimer, once a simple marker of fibrinolysis, has evolved into a multifaceted indicator in the realm of medicine. Its physiological role as a byproduct of clot dissolution is intertwined with its diagnostic significance in thrombotic events and cardiovascular diseases. Furthermore, emerging research is uncovering its involvement in inflammatory processes, broadening its clinical implications. By delving into the complexities of D-dimer, scientists and clinicians pave the way for a deeper understanding of coagulation disorders and associated conditions, driving advancements in diagnostics and therapies.

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Description:

IGF1 Gilthead Seabream Recombinant

Somatomedin C, IGF-I, IGFI.

Product # :

CYT-295

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Description

IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.IGF-1 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

Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.

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Introduction
The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.
Synonyms
Somatomedin C, IGF-I, IGFI.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 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
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK
Background
What is the molecular weight/Mw of IGF1 GILTHEAD SEABREAM Protein?
IGF1 GILTHEAD SEABREAM Protein has a total Mw of 7.54kDa.

What is the source or expression system of IGF1 GILTHEAD SEABREAM Protein?
Escherichia Coli.

What is the Purity of IGF1 GILTHEAD SEABREAM Protein?
IGF1 GILTHEAD SEABREAM Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 GILTHEAD SEABREAM Protein?
Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.

What is the amino acid sequence of IGF1 GILTHEAD SEABREAM Protein?
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK

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

What is the endotoxin level for IGF1 GILTHEAD SEABREAM Protein?
The endotoxin level is minimal, IGF1 GILTHEAD SEABREAM Protein was purified using conventional chromatography techniques.
Protein content
Somatomedin C quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.60 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). 2. Analysis by RP-HPLC, using a calibrated solution of IGF1 as a Reference Standard.

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Description:

Ribosomal Protein L35A Human Recombinant

Ribosomal Protein L35a, Cell Growth-Inhibiting Gene 33 Protein, 60S Ribosomal Protein L35a, DBA5, L35A.

Product # :

PRO-1703

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Description

RPL35A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.9kDa.RPL35A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RPL35A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Ribosomes, the organelles which catalyze protein synthesis, contain a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and nearly 80 structurally different proteins. RPL35A is a component of the 60S subunit of the ribosomal protein and a member of the L35AE family of ribosomal proteins. RPL35A is situated in the cytoplasm. The rat protein is known to bind to both initiator and elongator tRNAs, therefore, it is located at the P site, or P and A sites, of the ribosome. Though RPL35A was initially mapped to chromosome 18, it has been proven that it is located at 3q29-qter. Transcript variants utilizing alternative transcription initiation sites and alternative polyA signals exist. As is typical for genes encoding ribosomal proteins, there are several processed pseudogenes of this gene spread all over the genome.
Synonyms
Ribosomal Protein L35a, Cell Growth-Inhibiting Gene 33 Protein, 60S Ribosomal Protein L35a, DBA5, L35A.
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 MGSMSGRLWS KAIFAGYKRG LRNQREHTAL LKIEGVYARD ETEFYLGKRC AYVYKAKNNT VTPGGKPNKT RVIWGKVTRA HGNSGMVRAK FRSNLPAKAI GHRIRVMLYP SRI

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