Search: 1000 results found for "Ribosomal Protein"

Description:

Actin Related Protein 2/3 Complex, Subunit 2 Human Recombinant

ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.

Product # :

PRO-1418

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Description

ARPC2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300a.a) and having a molecular mass of 36.7kDa. ARPC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

ARPC2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Actin-related protein 2/3 complex subunit 2 (ARPC2), is a part of the Rho family of small GTPases and one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. Nevertheless, the exact role of the protein (the p34 subunit) has yet to be determined.
Synonyms
ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.
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 MGSMILLEVN NRIIEETLAL KFENAAAGNK PEAVEVTFAD FDGVLYHISN PNGDKTKVMV SISLKFYKEL QAHGADELLK RVYGSFLVNP ESGYNVSLLY DLENLPASKD SIVHQAGMLK RNCFASVFEK YFQFQEEGKE GENRAVIHYR DDETMYVESK KDRVTVVFST VFKDDDDVVI GKVFMQEFKE GRRASHTAPQ VLFSHREPPL ELKDTDAAVG DNIGYITFVL FPRHTNASAR DNTINLIHTF RDYLHYHIKC SKAYIHTRMR AKTSDFLKVL NRARPDAEKK EMKTITGKTF SSR.

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:

Outer Membrane Protein Treponema pallidum Recombinant

Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453

Product # :

TRP-255

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Description

Recombinant Treponema pallidum Outer Membrane Protein TP0453 has a Mw of 26kDa, and was purified from E. coli.The Recombinant Treponema pallidum Outer Membrane Protein TP0453 is fused to 6 amino acid His tag at its C terminal and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Treponema TP0453 solution contains 25mM K2CO3 with PBS.

Purity

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

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Introduction
Tp0453 is a carrier of lipids and glycolipids during outer membrane. Tp045 is hypothesized to be a new type of bacterial outer membrane protein, which reduces T.pallidum outer membrane permeability to nutrients while remaining inaccessible to antibodies. Tp0453 exhibited 100% specificity and sensitivity in reaction with syphilis patients’ sera, giving negative result with Lyme disease, relapsing-fever or leptospirosis patients’ sera.
Synonyms
Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Applications
Rapid test, Immunoassay.

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:

PEST proteolytic Signal Containing Nuclear Protein Human Recombinant

PEST proteolytic signal-containing nuclear protein, PCNP, PEST-containing nuclear protein.

Product # :

PRO-906

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Description

PCNP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178 a.a.) and having a molecular mass of 21.5kDa.PCNP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PCNP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PEST proteolytic signal containing nuclear protein (PCNP) is a nuclear protein involved in cell cycle regulation and tumorigenesis. The PCNP protein is ubiquitinated post-translationally by NIRF (an ubiquitin ligase). The PCNP exists as 3 isoforms produced by alternative splicing events.
Synonyms
PEST proteolytic signal-containing nuclear protein, PCNP, PEST-containing nuclear 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
MGSSHHHHHH SSGLVPRGSH MGSHMADGKA GDEKPEKSQR AGAAGGPEEE AEKPVKTKTV SSSNGGESSS RSAEKRSAEE EAADLPTKPT KISKFGFAIG SQTTKKASAI SIKLGSSKPK ETVPTLAPKT LSVAAAFNED EDSEPEEMPP EAKMRMKNIG RDTPTSAGPN SFNKGKHGFS DNQKLWERNI KSHLGNVHDQ DN.

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:

KIN Human Recombinant

BTCD, KIN17, KIN, Binding to curved DNA, antigenic determinant of recA protein homolog, DNA/RNA-binding protein KIN17.

Product # :

PRO-1275

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Description

KIN Human Recombinant produced in E. coli is a single polypeptide chain containing 416 amino acids (1-393) and having a molecular mass of 47.8 kDa.KIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The KIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
DNA/RNA-binding protein KIN17 (KIN17) is a nuclear protein which constructs intranuclear foci for the duration of proliferation and is reallocated in the nucleoplasm during the cell cycle. KIN17 is ubiqutiously expressed having the highest levels of expression in the muscle, heart and testis. SV40- altered fibroblasts overexpress KIN17, which interacts with Large T antigen and decreases T-antigen-dependent DNA replication.
Synonyms
BTCD, KIN17, KIN, Binding to curved DNA, antigenic determinant of recA protein homolog, DNA/RNA-binding protein KIN17.
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 MGSMGKSDFL TPKAIANRIK SKGLQKLRWY CQMCQKQCRD
ENGFKCHCMS ESHQRQLLLA SENPQQFMDY FSEEFRNDFL ELLRRRFGTK RVHNNIVYNE YISHREHIHM NATQWETLTD FTKWLGREGL CKVDETPKGW YIQYIDRDPE TIRRQLELEK
KKKQDLDDEE KTAKFIEEQV RRGLEGKEQE VPTFTELSRE NDEEKVTFNL SKGACSSSGA
TSSKSSTLGP SALKTIGSSA SVKRKESSQS STQSKEKKKK KSALDEIMEI EEEKKRTART
DYWLQPEIIV KIITKKLGEK YHKKKAIVKE VIDKYTAVVK MIDSGDKLKL DQTHLETVIP
APGKRILVLN GGYRGNEGTL ESINEKTFSA TIVIETGPLK GRRVEGIQYE DISKLA.

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:

Synaptosomal-associated protein 23 Human Recombinant

SNAP23A, SNAP23B, HsT17016, Synaptosomal-associated protein 23, Vesicle-membrane fusion protein SNAP-23, SNAP23.

Product # :

PRO-659

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Description

SNAP23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids and having a molecular mass of 23.3 kDa.

Source

Escherichia Coli.

Formulation

The protein solution contains 20mM Tris-HCl pH-8.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SNAP23 is a non-neuronal SNAP25 protein homologue and a target SNARE ubiquitously expressed on the plasma membrane and other intracellular membranes. SNAP23 is involved in exocytotic membrane fusion in most cells that do not express SNAP-25. SNAP23 is an essential component of the high affinity receptor for the general membrane fusion machinery and an crucial regulator of transport vesicle docking and fusion. SNAP23 is phosphorylated in platelets through cell activation during a protein kinase C-related mechanism at two or more sites. SNAP23, the ubiqitously expressed homologue of SNAP25, interacts directly with ubiquitous kinesin heavy chain (uKHC). SNAP-23 is expressed in human eosinophils and is a candidates for association with VAMP-2 during docking, which is followed by exocytosis.
Synonyms
SNAP23A, SNAP23B, HsT17016, Synaptosomal-associated protein 23, Vesicle-membrane fusion protein SNAP-23, SNAP23.
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
MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK TTWGDGGENS PCNVVSKQPG PVTNGQLQQP TTGAASGGYI KRITNDARED EMEENLTQVG SILGNLKDMA LNIGNEIDAQ NPQIKRITDK ADTNRDRIDI ANARAKKLID S.

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:

GTP-Binding Protein SAR1A Human Recombinant

GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.

Product # :

PRO-709

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Description

SAR1A Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids (1- 198 a.a.) and having a molecular mass of 24.5kDa.The SAR1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SAR1A solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SAR1A is a member of the small GTPase superfamily. SAR1A is a vital component of COPII vesicle coats involved in export of cargo from the ER (Endoplasmic Reticulum). The GTPase activity of SAR1A serves as a molecular switch to control protein-protein and protein-lipid interactions which dictate vesicle budding from the ER. SAR1A, while GDP-bound interacts with the membrane-bound exchange factor Sec12 and trades its bound GDP for GTP. SAR1A is also involved in the transport from the ER to the Golgi apparatus. SAR1A is required to maintain SEC16A localization at distinct locations on the ER membrane possibly by preventing its dissociation. SAR1A-GTP-dependent compilation of SEC16A on the ER membrane creates a structured scaffold defining endoplasmic reticulum exit sites.
Synonyms
GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.
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 MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLVE SKVELNALMT DETISNVPIL ILGNKIDRTD AISEEKLREI FGLYGQTTGK GNVTLKELNA RPMEVFMCSV LKRQGYGEGF RWLSQYID.

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:

Vesicle-associated membrane protein 5 Human Recombinant

VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.

Product # :

PRO-681

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Description

VAMP5 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 109 amino acids (1-72 a.a.) and having a molecular mass of 12.7 kDa.VAMP5 is fused to 37 amino acids His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The VAMP5 (0.5mg/ml) protein solution contains 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 5mM DTT, 0.5mM EDTA and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
VAMP5 is part of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. VAMP5 is involved is vesicle trafficking events that are associated with myogenesis.
Synonyms
VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAG IELERCQQQA NEVTEIMRNN FGKVLERGVK LAELQQRSDQ LLDMSSTFNK TTQNLAQKKC WENIRYRIC.

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:

Bone Morphogenetic Protein-7 Human Recombinant, Plant

Osteogenic Protein 1, BMP-7.

Product # :

CYT-039

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Description

Bone Morphogenetic Protein-7 Human Recombinant produced in Plant is a monomeric, glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 16.5kDa, and fused to a 6xHis-tag at the N-terminus. The BMP-7 is purified by proprietary chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

BMP-7 was lyophilized from a solution containing Tris-HCl 0.05M buffer at pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of BMP-7 was measured by its ability to induce alkaline phosphatase production by ATDC5 cells, ED₅₀ is less than 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
Synonyms
Osteogenic Protein 1, BMP-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP 7 Human 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
Lyophilized BMP-7 protein should be reconstituted in distilled water to a concentration of 50 ng/µl.
Amino Acid Sequence
HHHHHHSTGSKQRSQNRSKTPKNQEALRMANVAEN
SSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAY
YCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
CCAPTQLNAISVLYFDDSSVILKKYRNMVVRACGCH.
Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, Plant, Monomer, HEK
Abstract:
Welcome to our research paper exploring the incredible world of Bone Morphogenetic Protein-7 Human Recombinant, Plant, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this study, we embark on a captivating journey to unravel the wonders of BMP-7 HR and its significance in cellular differentiation. As a key member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR plays a pivotal role in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells, while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Step into the fascinating world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its crucial role in guiding cellular differentiation. Meet our trusted companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, paving the way for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatility, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR from plant sources opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.5kDa.

What is the source or expression system of BMP7 Protein?
Escherichia Coli.

What is the Purity of BMP7 Protein?
BMP7 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP7 Protein?
The biological activity of BMP-7 was measured by its ability to induce alkaline phosphatase production by ATDC5 cells, ED50 is less than 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

What is the amino acid sequence of BMP7 Protein?
HHHHHHSTGSKQRSQNRSKTPKNQEALRMANVAEN
SSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAY
YCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
CCAPTQLNAISVLYFDDSSVILKKYRNMVVRACGCH.

What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.

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Description:

Bactericidal/Permeability-Increasing Protein Human

Bactericidal/permeability-increasing protein, CAP 57.

Product # :

PRO-129

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Description

The native protein BPI is isolated from human buffy coats and has a molecular mass of 53kDa.

Formulation

BPI (1.15mg/ml) is supplied in 25mM Sodium Acetate pH-4.6.

Purity

Greater than 70% as determined by SDS-PAGE and capillary electrophoresis.

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Introduction
BPI encodes a lipopolysaccharide binding protein. BPI is related to human neutrophil granules and has bactericidal activity on gram-negative organisms.
Synonyms
Bactericidal/permeability-increasing protein, CAP 57.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

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

Description:

Minichromosome Maintenance Complex Component 7 Human Recombinant

Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.

Product # :

PRO-1847

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Description

MCM7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414) and having a molecular mass of 48.6 kDa. MCM7 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The MCM7 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.
Synonyms
Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.
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 MGSMVVATYT CDQCGAETYQ PIQSPTFMPL IMCPSQECQT NRSGGRLYLQ TRGSRFIKFQ EMKMQEHSDQ VPVGNIPRSI TVLVEGENTR IAQPGDHVSV TGIFLPILRT GFRQVVQGLL SETYLEAHRI VKMNKSEDDE SGAGELTREE LRQIAEEDFY EKLAASIAPE IYGHEDVKKA LLLLLVGGVD QSPRGMKIRG NINICLMGDP GVAKSQLLSY IDRLAPRSQY TTGRGSSGVG LTAAVLRDSV SGELTLEGGA LVLADQGVCC IDEFDKMAEA DRTAIHEVME QQTISIAKAG ILTTLNARCS ILAAANPAYG RYNPRRSLEQ NIQLPAALLS RFDLLWLIQD RPDRDNDLRL AQHITYVHQH SRQPPSQFEP LDMKLMRRYI AMCREKQPMV PESLADYITA AYVEMRR

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Description:

Centromere Protein-H Human Recombinant

Centromere protein H, Interphase centromere complex protein 35, CENP-H, NNF1, PMF1, ICEN35, Kinetochore protein CENP-H.

Product # :

PRO-966

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Description

CENPH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (136-247) and having a molecular mass of 15.5 kDa.The CENPH is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CENPH 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
CENPH is a member of the centromere protein H family. CENPH protein is a component of the CENPA-NAC (nucleosome-associated) complex which has a vital part in assembly of kinetochore proteins. The CENPA-NAC complex utilizes the CENPA-CAD (nucleosome distal) complex and is involved in integration of freshly synthesized CENPA into centromeres.
Synonyms
Centromere protein H, Interphase centromere complex protein 35, CENP-H, NNF1, PMF1, ICEN35, Kinetochore protein CENP-H.
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 MLNKLIMKSQ QESWDLEEKL LDIRKKRLQL KQASESKLLE IQTEKNKQKI DLDSMENSER IKIIRQNLQM EIKITTVIQH VFQNLILGSK VNWAEDPALK EIVLQLEKNV DMM

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Description:

Centromere Protein-P Human Recombinant

Centromere protein P, CENP-P, CENPP.

Product # :

PRO-1784

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Description

CENPP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-288 a.a) and having a molecular mass of 35.3kDa.CENPP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Centromere protein P (CENPP) is component of the CENPA-CAD (nucleosome distal) complex, which is a complex recruited to centromeres and involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. CENPP protein is involved in incorporation of newly synthesized CENPA into centromeres by way of its interaction with the CENPA-NAC complex.
Synonyms
Centromere protein P, CENP-P, CENPP.
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 MDAELAEVRA LQAEIAALRR ACEDPPAPWE EKSRVQKSFQ AIHQFNLEGW KSSKDLKNQL GHLESELSFL STLTGINIRN HSKQTEDLTS TEMTEKSIRK VLQRHRLSGN CHMVTFQLEF QILEIQNKER LSSAVTDLNI IMEPTECSEL SEFVSRAEER KDLFMFFRSL HFFVEWFEYR KRTFKHLKEK YPDAVYLSEG PSSCSMGIRS ASRPGFELVI VWRIQIDEDG KVFPKLDLLT KVPQRALELD KNRAIETAPL SFRTLVGLLG IEAALESLIK SLCAEENN.

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:

Cell Division Cycle 123 Human Recombinant

C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

Product # :

PRO-1463

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Description

CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.
Synonyms
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD

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:

Toll Interacting Protein 1 Human Recombinant

Toll-interacting protein, TOLLIP, IL-1RAcPIP.

Product # :

PRO-228

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Description

TOLLIP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (1-274 a.a) and having a molecular mass of 32.4kDa.TOLLIP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TOLLIP protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.2M NaCl and 2mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Toll interacting protein (TOLLIP) is an inhibitory adaptor protein within Toll-like receptors. The TLR pathway is a part of the innate immune system which recognizes structurally conserved molecular patterns of microbial pathogens, initiating an inflammatory immune response. Negative regulation of TLR signaling by TOLLIP might restrict the production of proinflammatory mediators during inflammation and infection. Furthermore, TOLLIP forms a complex with Tom1 to regulate endosomal transferring of ubiquitinated proteins.
Synonyms
Toll-interacting protein, TOLLIP, IL-1RAcPIP.
Physical Appearance
Sterile Filtered colorless solution.
Stability
TOLLIP Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATTVSTQRG PVYIGELPQD FLRITPTQQQ RQVQLDAQAA QQLQYGGAVG TVGRLNITVV QAKLAKNYGM TRMDPYCRLR LGYAVYETPT AHNGAKNPRW NKVIHCTVPP GVDSFYLEIF DERAFSMDDR IAWTHITIPE SLRQGKVEDK WYSLSGRQGD DKEGMINLVM SYALLPAAMV MPPQPVVLMP TVYQQGVGYV PITGMPAVCS PGMVPVALPP AAVNAQPRCS EEDLKAIQDM FPNMDQEVIR SVLEAQRGNK DAAINSLLQM GEEP.

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:

Mitochondrial Antiviral Signaling Protein Human Recombinant

CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

Product # :

PRO-1351

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Description

MAVS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 536 amino acids (1-513) and having a molecular mass of 55.9 kDa. MAVS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MAVS solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Mitochondrial antiviral signaling protein (MAVS) is vital for innate immune defense against viruses. MAVS is an intermediary protein essential in the virus-triggered IFN-beta signaling pathways. MAVS is involved in activation of transcription factors that regulate expression of IFN-beta and contributes to antiviral immunity.
Synonyms
CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.
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 MGSMPFAEDK TYKYICRNFS NFCNVDVVEI LPYLPCLTAR DQDRLRATCT LSGNRDTLWH LFNTLQRRPG WVEYFIAALR GCELVDLADE VASVYQSYQP RTSDRPPDPL EPPSLPAERP GPPTPAAAHS IPYNSCREKE PSYPMPVQET QAPESPGENS EQALQTLSPR AIPRNPDGGP LESSSDLAAL SPLTSSGHQE QDTELGSTHT AGATSSLTPS RGPVSPSVSF QPLARSTPRA SRLPGPTGSV VSTGTSFSSS SPGLASAGAA EGKQGAESDQ AEPIICSSGA EAPANSLPSK VPTTLMPVNT VALKVPANPA SVSTVPSKLP TSSKPPGAVP SNALTNPAPS KLPINSTRAG MVPSKVPTSM VLTKVSASTV PTDGSSRNEE TPAAPTPAGA TGGSSAWLDS SSENRGLGSE LSKPGVLASQ VDSPFSGCFE DLAISASTSL GMGPCHGPEE NEYKSEGTFG IHVAENPSIQ LLEGNPGPPA DPDGGPRPQA DRKFQEREVP CHRPSP.

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:

TRAF-Interacting Protein with Forkhead-Associated Domain Human Recombinant

TRAF-interacting protein with FHA domain-containing protein A, Putative MAPK-activating protein PM14, Putative NF-kappa-B-activating protein 20, TRAF2-binding protein, TIFA, T2BP, T6BP, TIFAA.

Product # :

PRO-1041

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Description

TIFA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-184 a.a.) and having a molecular mass of 24kDa.TIFA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TIFA protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TRAF-interacting protein with FHA domain-containing protein A (TIFA) is an adapter protein that mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, triggering the downstream activation of NF-kappa-B and AP-1 pathways. The TIFA protein stimulates the oligomerization and polyubiquitination of TRAF6, leading to the activation of TAK1 and IKK through a proteasome-independent mechanism.
Synonyms
TRAF-interacting protein with FHA domain-containing protein A, Putative MAPK-activating protein PM14, Putative NF-kappa-B-activating protein 20, TRAF2-binding protein, TIFA, T2BP, T6BP, TIFAA.
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 MGSHMTSFED ADTEETVTCL QMTVYHPGQL QCGIFQSISF NREKLPSSEV VKFGRNSNIC HYTFQDKQVS RVQFSLQLFK KFNSSVLSFE IKNMSKKTNL IVDSRELGYL NKMDLPYRCM VRFGEYQFLM EKEDGESLEF FETQFILSPR SLLQENNWPP HRPIPEYGTY SLCSSQSSSP TEMDENES.

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:

Proteasome Subunit Beta Type 5 Human Recombinant

Proteasome subunit beta type-5, Macropain epsilon chain, Multicatalytic endopeptidase complex epsilon chain, Proteasome chain 6, Proteasome epsilon chain, Proteasome subunit MB1, Proteasome subunit X, PSMB5, LMPX, MB1, X, MGC104214.

Product # :

ENZ-050

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Description

PSMB5 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 241 amino acids (60-263 a.a.) and having a molecular mass of 26.7kDa. The PSMB5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PSMB5 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 5mM DTT and 0.2M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
PSMB5 belongs to the proteasome B-type family that has a 20S core beta subunit in the proteasome. This catalytic subunit is not present in the immunoproteasome and is substituted by catalytic subunit 3i (proteasome beta 8 subunit). A fundamental function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB5 exhibits an ATP dependent proteolytic activity and is involved in an ATP/ubiquitin dependent non lysosomal proteolytic pathway.
Synonyms
Proteasome subunit beta type-5, Macropain epsilon chain, Multicatalytic endopeptidase complex epsilon chain, Proteasome chain 6, Proteasome epsilon chain, Proteasome subunit MB1, Proteasome subunit X, PSMB5, LMPX, MB1, X, MGC104214.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMTTT LAFKFRHGVI VAADSRATAG AYIASQTVKK VIEINPYLLG TMAGGAADCS FWERLLARQC RIYELRNKER ISVAAASKLL ANMVYQYKGM GLSMGTMICG WDKRGPGLYY VDSEGNRISG ATFSVGSGSV YAYGVMDRGY SYDLEVEQAY DLARRAIYQA TYRDAYSGGA VNLYHVREDG WIRVSSDNVA DLHEKYSGST P.

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

Description:

Argonaute 2 Human Recombinant

Protein argonaute-2, Argonaute2, hAgo2, Argonaute RISC catalytic component 2, Eukaryotic translation initiation factor 2C 2, eIF-2C 2, eIF2C 2, PAZ Piwi domain protein, PPD, AGO2, EIF2C2, Protein slicer.

Product # :

PRO-2577

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Description

AGO2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 1-859) containing 869 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 98.4kDa (calculated).

Source

Escherichia Coli.

Formulation

AGO2 filltered solution in 50mM acetate buffer, pH 4.0 and 20% (w/v) glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The Argonaute protein is part of the RISC or RNA-induced silencing complex, as so, the protein has a key part in the slicing processes of RNA. The RNA interference (RNAi) is being held by RISC. Small non-coding RNA fragments bond to the Argonaute proteins, through base pairing, eventually leads to the cleavage of messenger RNA or translation suppression.
Synonyms
Protein argonaute-2, Argonaute2, hAgo2, Argonaute RISC catalytic component 2, Eukaryotic translation initiation factor 2C 2, eIF-2C 2, eIF2C 2, PAZ Piwi domain protein, PPD, AGO2, EIF2C2, Protein slicer.
Physical Appearance
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
MKHHHHHHAS MYSGAGPALA PPAPPPPIQG YAFKPPPRPD FGTSGRTIKL QANFFEMDIP KIDIYHYELD IKPEKCPRRV NREIVEHMVQ HFKTQIFGDR KPVFDGRKNL YTAMPLPIGR DKVELEVTLP GEGKDRIFKV SIKWVSCVSL QALHDALSGR LPSVPFETIQ ALDVVMRHLP SMRYTPVGRS FFTASEGCSN PLGGGREVWF GFHQSVRPSL WKMMLNIDVS ATAFYKAQPV IEFVCEVLDF KSIEEQQKPL TDSQRVKFTK EIKGLKVEIT HCGQMKRKYR VCNVTRRPAS HQTFPLQQES GQTVECTVAQ YFKDRHKLVL RYPHLPCLQV GQEQKHTYLP LEVCNIVAGQ RCIKKLTDNQ TSTMIRATAR SAPDRQEEIS KLMRSASFNT DPYVREFGIM VKDEMTDVTG RVLQPPSILY GGRNKAIATP VQGVWDMRNK QFHTGIEIKV WAIACFAPQR QCTEVHLKSF TEQLRKISRD AGMPIQGQPC FCKYAQGADS VEPMFRHLKN TYAGLQLVVV ILPGKTPVYA EVKRVGDTVL GMATQCVQMK NVQRTTPQTL SNLCLKINVK LGGVNNILLP QGRPPVFQQP VIFLGADVTH PPAGDGKKPS IAAVVGSMDA HPNRYCATVR VQQHRQEIIQ DLAAMVRELL IQFYKSTRFK PTRIIFYRDG VSEGQFQQVL HHELLAIREA CIKLEKDYQP GITFIVVQKR HHTRLFCTDK NERVGKSGNI PAGTTVDTKI THPTEFDFYL CSHAGIQGTS RPSHYHVLWD DNRFSSDELQ ILTYQLCHTY VRCTRSVSIP APAYYAHLVA FRARYHLVDK EHDSAEGSHT SGQSNGRDHQ ALAKAVQVHQ DTLRTMYFA.

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:

Yersinia Enterocolitica (O:9) YopH Recombinant

Product # :

PRO-2275

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Description

Recombinant Yersinia Enterocolitica (O:9) YopH produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 52,311 Dalton. Y.Enterocolitica (O:9) YopH is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Y.Enterocolitica (O:9) YopH is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.
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- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.

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:

Bridging Integrator 1 Human Recombinant

AMPH2, AMPHL, MGC10367, SH3P9, Amphiphysin II.

Product # :

PRO-546

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Description

BIN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 459 amino acids (1-439 a.a) and having a molecular mass of 50.4 kDa. The BIN1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BIN1 protein solution (1mg/ml) containing 20mM Tris buffer pH-8, 1mM DTT & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
BIN1 is a nucleocytoplasmic adaptor protein, one of which was primarily identified as MYC-interacting protein having the characteristics of a tumor suppressor. BIN1 protein interacts with and inhibits the oncogenic activity of the myc oncoprotein that is a key player in many human cancers. The absence of Bin1 contributes to growth deregulation in cancer cells in carcinoma of the breast, colon, lung, cervix, prostate and liver.
Synonyms
AMPH2, AMPHL, MGC10367, SH3P9, Amphiphysin II.
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 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE KQHGSNTFTV KAQPSDNAPA KGNKSPSPPD GSPAATPEIR VNHEPEPAGG ATPGATLPKS PSQPAEASEV AGGTQPAAGA QEPGETAASE AASSSLPAVV VETFPATVNG TVEGGSGAGR LDLPPGFMFK VQAQHDYTAT DTDELQLRAG DVVLVIPFQN PEEQDEGWLM GVKESDWNQH KELEKCRGVF PENFTERVP.

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

Description:

Epidermal Growth Factor Rat

Urogastrone, URG, EGF.

Product # :

CYT-556

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Description

Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Adult Male Rat Submandibular Glands.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

Purity

Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.15kDa.

What is the source or expression system of EGF RAT Protein?
Adult Male Rat Submandibular Glands.

What is the Purity of EGF RAT Protein?
EGF RAT Protein is >99% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of EGF RAT Protein?
EGF RAT Protein is composed from 53 amino acids.

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

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

Retinol Binding Protein-4, Mouse Anti Human

Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

Product # :

ANT-371

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
Retinol binding protein 4(RBP4) belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. This protein was found to be expressed and secreted by adipose tissue, and was strongly associated with insulin resistance. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli. RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the rbp-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.
Synonyms
Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
Immunogen
Anti-human RBP4 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human RBP4 amino acids 19-201 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
PAT2B4AT.
Applications
RBP4 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1000. Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
RBP4 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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:

Small Nuclear Ribonucleoprotein Polypeptide D3 Human Recombinant, Sf9

Small nuclear ribonucleoprotein D3 polypeptide 18kDa, Sm-D3, snRNP core protein D3.

Product # :

PRO-996

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Description

SNRPD3 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 18 KDa. SNRPD3 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

SNRPD3 is supplied in 20mM HEPES buffer pH-7.5, 400mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
SNRPD3 is a small nuclear ribonucleoprotein (snRNPs) that contains the spliceosome in eukaryotes. SNRPD3 is essential for pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis. Alternative splicing happens in this locus and two transcript variants encoding the same protein were branded.
Synonyms
Small nuclear ribonucleoprotein D3 polypeptide 18kDa, Sm-D3, snRNP core protein D3.
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-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative samples).
coating concentration
0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
Applications
Western blot with anti-Sm positive patient sera.

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:

Bone Morphogenetic Protein-7 Human Recombinant, His Tag

Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.

Product # :

CYT-629

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sds-page

Description

BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
Synonyms
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
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 avoid freeze thaw cycles.
Amino Acid Sequence
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK
Abstract:
Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.8kDa.

What is the source or expression system of BMP7 Protein?
Escherichia Coli.

What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.

What is the amino acid sequence of BMP7 Protein?
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.

What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.

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

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